Sandbox Reserved 1561 - Revision history

Student at 21:13, 9 December 2019

Student — Mon, 09 Dec 2019 21:13:10 GMT

←Older revision		Revision as of 21:13, 9 December 2019
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	{{Sandbox_Reserved_BHall_Chem351_F19}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->		{{Sandbox_Reserved_BHall_Chem351_F19}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
-	==Bap1 from ''Vibrio ~~cholera~~'' plays a crucial role in biofilm binding affinity==	+	==Bap1 from ''Vibrio cholerae'' plays a crucial role in biofilm binding affinity==
	<StructureSection load='6MLT' size='400' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='6MLT' size='400' side='right' caption='Caption for this structure' scene=''>

Student at 21:08, 9 December 2019

Student — Mon, 09 Dec 2019 21:08:53 GMT

←Older revision		Revision as of 21:08, 9 December 2019
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	== References ==		== References ==
	<references/>		<references/>
-	3. “Travelers' Health.” Centers for Disease Control and Prevention, Centers for Disease Control and Prevention, 3 Oct. 2019, wwwnc.cdc.gov/travel/diseases/cholera.
-
-	4. Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.

Student at 07:19, 9 December 2019

Student — Mon, 09 Dec 2019 07:19:50 GMT

←Older revision		Revision as of 07:19, 9 December 2019
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	<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>		<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

-	<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate ~~bonding~~. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>	+	<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate binding. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>

	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site. The active site of Bap1 is outside of its central cavity of the eight-bladed beta-propeller and doesn't yield a catalytic triad.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>		<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site. The active site of Bap1 is outside of its central cavity of the eight-bladed beta-propeller and doesn't yield a catalytic triad.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

Student at 07:03, 9 December 2019

Student — Mon, 09 Dec 2019 07:03:59 GMT

←Older revision		Revision as of 07:03, 9 December 2019
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	== Function(s) and Biological Relevance ==		== Function(s) and Biological Relevance ==
-	Bap1 (Biofilm-Associated protein 1) is an extracellular matrix protein from the bacterium Vibrio cholerae that aids in biofilm architecture and adhesion affinity to living surfaces. <scene name='82/823085/6mlt_cartoon_view/3'>Bap1 Cartoon View</scene> Bap1 is also responsible for the biofilm resistance in aqueous environments, acidic conditions, antibiotics and immune systems making the V. cholerae biofilm very versatile and difficult to eradicate. Vibrio cholerae biofilms are made up of Vibrio polysaccharides, nucleic acids and matrix proteins RBmA, RbmC, and Bap1. V. cholerae biofilms are linked to increased transmission, virulence and resistance to various environments, which resulted in pandemic cholera. The biofilm resistance and adhesion affinity promote survival in a multitude of environments including mammalian stomachs. The increased resistance and adhesion affinity increase the virulence of the bacterium resulting in a greater probability of contraction, infection and disease.	+	Bap1 (Biofilm-Associated protein 1) is an extracellular matrix protein from the bacterium ''Vibrio cholerae'' that aids in biofilm architecture and adhesion affinity to living surfaces. <scene name='82/823085/6mlt_cartoon_view/3'>Bap1 Cartoon View</scene> Bap1 is also responsible for the biofilm resistance in aqueous environments, acidic conditions, antibiotics and immune systems making the V. cholerae biofilm very versatile and difficult to eradicate. Vibrio cholerae biofilms are made up of Vibrio polysaccharides, nucleic acids and matrix proteins RBmA, RbmC, and Bap1. ''V. cholerae'' biofilms are linked to increased transmission, virulence and resistance to various environments, which resulted in pandemic cholera. The biofilm resistance and adhesion affinity promote survival in a multitude of environments including mammalian stomachs. The increased resistance and adhesion affinity increase the virulence of the bacterium resulting in a greater probability of contraction, infection and disease.

	== Broader Implications ==		== Broader Implications ==
-	It is important for medical professionals and scientists alike to understand how Vibrio cholerae interact with the host they are infecting. “Cholera is a disease spread by drinking water or eating food contaminated with cholera bacteria. ”The main implication cholera causes in humans is dehydration from loose stools. Pushing fluids to maintain hydration will lower your risk of death below 1%. The main implication of treating cholera is breaking down the V. cholerae biofilms which are resistant to antibiotics, stomach acid and antibiotics. Understanding how to break down this resistant biofilm could help many 3rd world countries and travelers avoid illness. <ref>“Travelers' Health.” Centers for Disease Control and Prevention, Centers for Disease Control and Prevention, 3 Oct. 2019, wwwnc.cdc.gov/travel/diseases/cholera.</ref>	+	It is important for medical professionals and scientists alike to understand how ''Vibrio cholerae'' interact with the host they are infecting. “Cholera is a disease spread by drinking water or eating food contaminated with cholera bacteria. ”The main implication cholera causes in humans is dehydration from loose stools. Pushing fluids to maintain hydration will lower your risk of death below 1%. The main implication of treating cholera is breaking down the ''V. cholerae'' biofilms which are resistant to antibiotics, stomach acid and antibiotics. Understanding how to break down this resistant biofilm could help many 3rd world countries and travelers avoid illness. <ref>“Travelers' Health.” Centers for Disease Control and Prevention, Centers for Disease Control and Prevention, 3 Oct. 2019, wwwnc.cdc.gov/travel/diseases/cholera.</ref>

	== Structural highlights and structure-function relationships ==		== Structural highlights and structure-function relationships ==
-	<scene name='82/823085/Tertiary_structure_view/1'> Tertiary Structure View</scene> Bap1 from V. cholerae is composed of a beta-prism that attaches to blade six of the eight-bladed beta-propeller. The beta-prism is an accessory domain to the eight-bladded beta-propeller domain, these two domains make up the tertiary structure of the protein.	+	<scene name='82/823085/Tertiary_structure_view/1'> Tertiary Structure View</scene> Bap1 from ''V. cholerae'' is composed of a beta-prism that attaches to blade six of the eight-bladed beta-propeller. The beta-prism is an accessory domain to the eight-bladded beta-propeller domain, these two domains make up the tertiary structure of the protein.

	<scene name='82/823085/Major_secondary_structure_view/1'> Major Secondary Structures </scene> of Bap1 can been viewed in the beta-propeller and throughout the protein as beta-sheets. Shown in red are the four anti-parallel beta-sheets that construct each blade of the eight-bladed beta-propeller of Bap1. <scene name='82/823085/Full_secondary_structure_view/1'>Full Secondary Structure View of Bap1</scene> shown in yellow are the beta-strands and shown in purple are the alpha-helix that make up Bap1.		<scene name='82/823085/Major_secondary_structure_view/1'> Major Secondary Structures </scene> of Bap1 can been viewed in the beta-propeller and throughout the protein as beta-sheets. Shown in red are the four anti-parallel beta-sheets that construct each blade of the eight-bladed beta-propeller of Bap1. <scene name='82/823085/Full_secondary_structure_view/1'>Full Secondary Structure View of Bap1</scene> shown in yellow are the beta-strands and shown in purple are the alpha-helix that make up Bap1.
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	== Energy Transformation ==		== Energy Transformation ==
-	Bap1 does not transform energy as its main purpose is adhesion, solubility and architecture to aid in in the virulence of the bacteria Vibrio cholerae.	+	Bap1 does not transform energy as its main purpose is adhesion, solubility and architecture to aid in in the virulence of the bacteria, ''Vibrio cholerae''.

	== References ==		== References ==

Student at 07:00, 9 December 2019

Student — Mon, 09 Dec 2019 07:00:47 GMT

←Older revision		Revision as of 07:00, 9 December 2019
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	== Energy Transformation ==		== Energy Transformation ==
-	Bap1 does not transform energy as its main purpose is ~~binding~~ and ~~promote structural integrity~~ of the ''Vibrio cholerae~~'' biofilm~~.	+	Bap1 does not transform energy as its main purpose is adhesion, solubility and architecture to aid in in the virulence of the bacteria Vibrio cholerae.

	== References ==		== References ==

Student at 06:59, 9 December 2019

Student — Mon, 09 Dec 2019 06:59:09 GMT

←Older revision		Revision as of 06:59, 9 December 2019
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	<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>		<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>
-
-	<scene name='82/823085/Active_binding_sites/1'> Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.

	<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate bonding. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>		<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate bonding. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>

-	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site.	+	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site. The active site of Bap1 is outside of its central cavity of the eight-bladed beta-propeller and doesn't yield a catalytic triad.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

	<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>		<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

Student at 06:55, 9 December 2019

Student — Mon, 09 Dec 2019 06:55:41 GMT

←Older revision		Revision as of 06:55, 9 December 2019
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	<scene name='82/823085/Isolated_beta-prism_view/1'> Beta-Prism View</scene> "The Bap1 Beta-prism falls into the jacalin-related (JRL) protein family, which consists of a pseudo-3-fold arrangement of Greek key motifs." <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> The beta-prism is located on blade six of the beta-propeller of Bap1 from V. cholerae. Bap1 beta-prism binds carbohydrate ligands along with citrate ions at a single sugar site. This binding process contributes to the crystal structure of Bap1.		<scene name='82/823085/Isolated_beta-prism_view/1'> Beta-Prism View</scene> "The Bap1 Beta-prism falls into the jacalin-related (JRL) protein family, which consists of a pseudo-3-fold arrangement of Greek key motifs." <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> The beta-prism is located on blade six of the beta-propeller of Bap1 from V. cholerae. Bap1 beta-prism binds carbohydrate ligands along with citrate ions at a single sugar site. This binding process contributes to the crystal structure of Bap1.

-	<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.	+	<scene name='82/823085/Sodium_calcium_ion_view/1'> Sodium Calcium Ion View</scene> Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

	<scene name='82/823085/Active_binding_sites/1'> Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.		<scene name='82/823085/Active_binding_sites/1'> Active Binding Sites</scene> Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller. There seems to be no catalytic triad associated within Bap1.

Student at 06:51, 9 December 2019

Student — Mon, 09 Dec 2019 06:51:48 GMT

←Older revision		Revision as of 06:51, 9 December 2019
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	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site.		<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site.

-	<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.	+	<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref>

	<scene name='82/823085/Asp348/1'>Asp348</scene> is the key amino acid residue of carbohydrate bonding.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref> The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.		<scene name='82/823085/Asp348/1'>Asp348</scene> is the key amino acid residue of carbohydrate bonding.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref> The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.

Student at 06:50, 9 December 2019

Student — Mon, 09 Dec 2019 06:50:12 GMT

←Older revision		Revision as of 06:50, 9 December 2019
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	<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.		<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.

-	<scene name='82/823085/Asp348/1'>Asp348</scene>is the key residue of carbohydrate bonding. The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.	+	<scene name='82/823085/Asp348/1'>Asp348</scene> is the key amino acid residue of carbohydrate bonding.<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref> The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.

	== Energy Transformation ==		== Energy Transformation ==

Student at 06:47, 9 December 2019

Student — Mon, 09 Dec 2019 06:47:20 GMT

←Older revision		Revision as of 06:47, 9 December 2019
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	<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate bonding. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>		<scene name='82/823085/Key_bap1_residues/1'> Key Bap1 Residues</scene> include Asp348, Trp986, Tyr894, Trp948, Asn871, Asp853 and Phe850. These key residues are located in the beta-prism of the Bap1 and are associated with carbohydrate bonding. <ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019</ref>

-	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site.	+	<scene name='82/823085/Bap1_active_site/1'>Bap1 Active Site</scene> is within the beta-prism composed of Gly344, Ala345, Val346, Lys501(Hydrogen bonding), Asp348 and His500(Van Der Waals interactions).<ref>Kaus, Katherine, et al. The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio Cholerae Provides Insights into Bacterial Biofilm Adhesion. The American Society for Biochemistry and Molecular Biology, 2019.</ref> Within the active site of Bap1, citrate and carbohydrates competitively bind for the same sugar binding site and citrate was necessary for obtaining the correct crystal form and contacts with its crystal environment surrounding the binding site.

	<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.		<scene name='82/823085/Citrate_anion/2'>Citrate anion</scene> The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.