Sandbox Reserved 1467 - Revision history

Amber Rupiper at 21:54, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 21:54:45 GMT

←Older revision		Revision as of 21:54, 1 December 2018
Line 18:		Line 18:
	A loop of Ser-785–Thr-786 –Pro-787 and two arginine residues (Arg-856 and Arg-999) are in the active site. Arg-856 and Arg-999, were found to be necessary		A loop of Ser-785–Thr-786 –Pro-787 and two arginine residues (Arg-856 and Arg-999) are in the active site. Arg-856 and Arg-999, were found to be necessary
	for the activity of Obc 1, showing that the two residues could serve as an oxyanion binding site in Obc1. The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		for the activity of Obc 1, showing that the two residues could serve as an oxyanion binding site in Obc1. The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.
-	The <scene name='79/799595/786936/2'>interaction between Thr-786 and Ser-936 </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/2'>crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.	+	The <scene name='79/799595/786936/2'>interaction between Thr-786 and Ser-936 </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/4'> crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.

	For kinetic conditions, C6-CoA adduct was found to be produced from ObcA. It was stable and could not be converted into CoA in the absence of Obc1, meaning the formation of CoA from the adduct is enzyme-dependent. The activity of Obc1 was measured in two different ways, both by the production of different products. In both experiments, the reaction mixture contained Co2+ ion as the most effective ion for ObcA activity <ref name="rasmol"/>.		For kinetic conditions, C6-CoA adduct was found to be produced from ObcA. It was stable and could not be converted into CoA in the absence of Obc1, meaning the formation of CoA from the adduct is enzyme-dependent. The activity of Obc1 was measured in two different ways, both by the production of different products. In both experiments, the reaction mixture contained Co2+ ion as the most effective ion for ObcA activity <ref name="rasmol"/>.

Amber Rupiper at 21:43, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 21:43:41 GMT

←Older revision		Revision as of 21:43, 1 December 2018
Line 18:		Line 18:
	A loop of Ser-785–Thr-786 –Pro-787 and two arginine residues (Arg-856 and Arg-999) are in the active site. Arg-856 and Arg-999, were found to be necessary		A loop of Ser-785–Thr-786 –Pro-787 and two arginine residues (Arg-856 and Arg-999) are in the active site. Arg-856 and Arg-999, were found to be necessary
	for the activity of Obc 1, showing that the two residues could serve as an oxyanion binding site in Obc1. The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		for the activity of Obc 1, showing that the two residues could serve as an oxyanion binding site in Obc1. The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.
-	The <scene name='79/799595/786936/1'>interaction between Thr-786 and Ser-936 ~~(red)~~ </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/2'>crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.	+	The <scene name='79/799595/786936/2'>interaction between Thr-786 and Ser-936 </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/2'>crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.

	For kinetic conditions, C6-CoA adduct was found to be produced from ObcA. It was stable and could not be converted into CoA in the absence of Obc1, meaning the formation of CoA from the adduct is enzyme-dependent. The activity of Obc1 was measured in two different ways, both by the production of different products. In both experiments, the reaction mixture contained Co2+ ion as the most effective ion for ObcA activity <ref name="rasmol"/>.		For kinetic conditions, C6-CoA adduct was found to be produced from ObcA. It was stable and could not be converted into CoA in the absence of Obc1, meaning the formation of CoA from the adduct is enzyme-dependent. The activity of Obc1 was measured in two different ways, both by the production of different products. In both experiments, the reaction mixture contained Co2+ ion as the most effective ion for ObcA activity <ref name="rasmol"/>.

Amber Rupiper at 21:32, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 21:32:49 GMT

←Older revision		Revision as of 21:32, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) shown is glycerol, which is bound to the Obc 1 C-domain <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/3'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) shown is glycerol, which is bound to the Obc 1 C-domain <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/3'>catalytic triad</scene>. The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
-	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.	+	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
-	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.	+	A loop of Ser-785–Thr-786 –Pro-787 and two arginine residues (Arg-856 and Arg-999) are in the active site. Arg-856 and Arg-999, were found to be necessary
		+	for the activity of Obc 1, showing that the two residues could serve as an oxyanion binding site in Obc1. The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.
	The <scene name='79/799595/786936/1'>interaction between Thr-786 and Ser-936 (red) </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/2'>crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.		The <scene name='79/799595/786936/1'>interaction between Thr-786 and Ser-936 (red) </scene> was found to be important for maintaining the structural integrity of a Ser-785–Thr-786 –Pro-787 loop near catalytic Ser-935 <ref name="rasmol"/>. The catalytic triad is located in the loop region, and these residues are clustered in a <scene name='79/799595/Catalytic_triad/2'>crevice (navy)</scene> in the C-domain, and their relative locations are conserved in other alpha/beta hydrolase <ref>PMID:10607665</ref>.

Amber Rupiper at 21:03, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 21:03:12 GMT

←Older revision		Revision as of 21:03, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) shown is glycerol, which is bound to the Obc 1 C-domain <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) shown is glycerol, which is bound to the Obc 1 C-domain <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/3'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.

Amber Rupiper at 20:58, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:58:50 GMT

←Older revision		Revision as of 20:58, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) is a glycerol bound ~~structure of Obc1~~ <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) shown is glycerol, which is bound to the Obc 1 C-domain <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.

Amber Rupiper at 20:56, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:56:47 GMT

←Older revision		Revision as of 20:56, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/2'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.

Amber Rupiper at 20:51, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:51:25 GMT

←Older revision		Revision as of 20:51, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/2'>space-filling view of the structure</scene> it is hard to distinguish between the different parts of the protein. The red balls in this view represent oxygen molecules. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.

Amber Rupiper at 20:47, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:47:05 GMT

←Older revision		Revision as of 20:47, 1 December 2018
Line 14:		Line 14:
	== Structural highlights ==		== Structural highlights ==
	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).		The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
-	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, ~~Obc1~~, mediate oxalogenesis. The N-domain consists of an ~~ObcB~~ activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.	+	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, the N-domain (navy) and the C-Domain (gray). The two domains in this protein, Obc 1, mediate oxalogenesis. The N-domain consists of an Obc B activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and researchers decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain and is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.
	The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.		The C-domain consists of <scene name='79/799595/C_domain/1'>two structural subdomains</scene>. The first region (navy), Ser-740 to Gln-1106, and forms an alpha/beta hydrolase fold. The second subdomain (red), Arg-529 to Ala-739, is located over a concave region formed by an alpha/beta hydrolase fold, resulting in a crevice between the two regions. The second domain is referred to as the cap domain <ref name="rasmol"/>.

Amber Rupiper at 20:42, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:42:18 GMT

←Older revision		Revision as of 20:42, 1 December 2018
Line 13:		Line 13:

	== Structural highlights ==		== Structural highlights ==
-	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices, with some additional beta sheets.	+	The <scene name='79/799595/Secondary_structure/1'>secondary structure</scene> of this protein is made up of mostly alpha helices (pink), with some additional beta sheets (yellow).
	The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.		The <scene name='79/799595/Tertiary_structure/1'>tertiary structure</scene> of this protein has two domains, N-domain (navy) and C-Domain (gray). The two domains in this protein, Obc1, mediate oxalogenesis. The N-domain consists of an ObcB activity-exhibiting C-terminal region (Arg-529 to Gln-1106). It was found that there were no extensive interactions between the two domains, and decided to focus on the C-domain. The C-domain (Arg-530 to Gln-1106) has features common to canonical alpha/beta hydrolyses <ref name="rasmol"/>. When looking at the <scene name='79/799595/Space_fill/1'>space-filling view of structure </scene> it is hard to distinguish between the different parts of the protein. This view can give a better insight on the size, shape, and representation of the complete molecule. The protein seems to be <scene name='79/799595/Hydrophobic/1'>equal parts</scene> hydrophobic and hydrophilic. The <scene name='79/799595/Ligand/1'>ligand</scene> (C3 H8 O3) is a glycerol bound structure of Obc1 <ref name="rasmol"/>. Arg-935, His-1069, and Asp-997 are the residues that make up the <scene name='79/799595/Catalytic_triad/1'>catalytic triad</scene> The catalytic triad is located in the C-domain is crucial to oxalate production. A change in the catalytic triad would most likely result in loss of function of the protein <ref name="rasmol"/>.
	The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.		The <scene name='79/799595/Active_site/1'>active site</scene> of the C-domain in a crevice between the cap domain and the alpha/beta hydrolase fold, and the position of the catalytic Ser-935.

Amber Rupiper at 20:40, 1 December 2018

Amber Rupiper — Sat, 01 Dec 2018 20:40:11 GMT

←Older revision		Revision as of 20:40, 1 December 2018
Line 10:		Line 10:

	== Relevance ==		== Relevance ==
-	By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. A bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the ''Burkholderia'' species <ref name="rasmol"/>.	+	By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. This bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the ''Burkholderia'' species <ref name="rasmol"/>.

	== Structural highlights ==		== Structural highlights ==