Sandbox Reserved 1758 - Revision history

Isabella Gonzalez at 16:45, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 16:45:28 GMT

←Older revision		Revision as of 16:45, 13 December 2022
Line 13:		Line 13:
	== Important amino acids==		== Important amino acids==

-	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg ~~148~~ and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.	+	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with <scene name='93/934002/Arg_128/1'>Arg 128</scene> and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
	This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The <scene name='93/934002/Space-filling_view/1'>space-filling view</scene> of the protein shows the ligand covered by the enzyme with the polar end sticking out of the cavity.		This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The <scene name='93/934002/Space-filling_view/1'>space-filling view</scene> of the protein shows the ligand covered by the enzyme with the polar end sticking out of the cavity.

Isabella Gonzalez at 16:06, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 16:06:39 GMT

←Older revision		Revision as of 16:06, 13 December 2022
Line 15:		Line 15:
	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.		The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
-	This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The ~~PtoMBD homodimer has a calculated mass of 42,186 Da.~~	+	This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The <scene name='93/934002/Space-filling_view/1'>space-filling view</scene> of the protein shows the ligand covered by the enzyme with the polar end sticking out of the cavity.
-	~~This is a sample scene created with SAT to~~ <scene name="/12/~~3456/Sample~~/1">~~color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation~~</scene> of the protein~~. You can make your own scenes on SAT starting from scratch or loading and editing one~~ of ~~these sample scenes~~.	+

	</StructureSection>		</StructureSection>
	== References ==		== References ==
	<references/>		<references/>

Isabella Gonzalez at 15:57, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 15:57:49 GMT

←Older revision		Revision as of 15:57, 13 December 2022
Line 15:		Line 15:
	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.		The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
-	This enzyme is a homodimer, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.	+	This enzyme is a <scene name='93/934002/Homodimer/1'>homodimer</scene>, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.
	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Isabella Gonzalez at 08:16, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 08:16:08 GMT

←Older revision		Revision as of 08:16, 13 December 2022
Line 15:		Line 15:
	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.		The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
-	~~Secondary Structure~~	+	This enzyme is a homodimer, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.
-	~~PtoMBD~~ is a homodimer, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.	+
	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Isabella Gonzalez at 08:14, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 08:14:35 GMT

←Older revision		Revision as of 08:14, 13 December 2022
Line 16:		Line 16:
	== Structural highlights ==		== Structural highlights ==
	Secondary Structure		Secondary Structure
-	PtoMBD is a homodimer, chains A and B are two asymmetrical monomers that contain both alpha helices and beta sheets. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.	+	PtoMBD is a homodimer, chains A and B are two asymmetrical monomers that contain both <scene name='93/934002/Secondary_structure/1'>alpha helices and beta sheets</scene>. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.
	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Isabella Gonzalez at 06:49, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 06:49:49 GMT

←Older revision		Revision as of 06:49, 13 December 2022
Line 13:		Line 13:
	== Important amino acids==		== Important amino acids==

-	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a ~~fatty acid. Oleic Acid is an amphipathic~~ fatty acid. One end has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.	+	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. One end of Oleic Acid has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
	Secondary Structure		Secondary Structure

Isabella Gonzalez at 06:47, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 06:47:54 GMT

←Older revision		Revision as of 06:47, 13 December 2022
Line 12:		Line 12:
	''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.		''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.
	== Important amino acids==		== Important amino acids==
-	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.<scene name='93/934002/Ligand/2'>ligand</scene>	+
		+	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.The internal surface of the cavity contains hydrophobic amino acid residues. The opening of the cavity holds charged or polar residues including Lys 94, Tyr 99, Arg 128, and Glu 138. This suggests an amphipathic <scene name='93/934002/Ligand/2'>ligand</scene>, such as Oleic Acid, a fatty acid. Oleic Acid is an amphipathic fatty acid. One end has a carboxylic acid which has a hydrogen bond with Arg 148 and a water molecule. The Oleic Acid chain of carbons is surrounded by non-polar amino acids such as valine.
	== Structural highlights ==		== Structural highlights ==
	Secondary Structure		Secondary Structure

Isabella Gonzalez at 06:30, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 06:30:04 GMT

←Older revision		Revision as of 06:30, 13 December 2022
Line 15:		Line 15:
	== Structural highlights ==		== Structural highlights ==
	Secondary Structure		Secondary Structure
-	PtoMBD is a homodimer, chains A and B are two asymmetrical monomers that contain both alpha helices and beta sheets. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.	+	PtoMBD is a homodimer, chains A and B are two asymmetrical monomers that contain both alpha helices and beta sheets. The chains are nearly identical and contain 12 alpha helices and 12 beta sheets. The outer surface is framed by an antiparallel beta-sheet that is composed of β6, β4,β1, and β12 followed along with the β5 strand. Other antiparallel beta-sheets include the formation of β2, β3, β7, β8 and β9, β11, and β10 strands. These two beta-sheets alongside α1, α8, α9, α10, α11, and α12 helices form the floor of the enzyme as well as a large cleft of the substrate-binding sites. The upper domain of the site is formed of α2, α3, α4, α5, α6, and α7 helices and β5, β6, β4, β1, β12.There is a resemblance to homologous decarboxylases seen in the GHMP kinases superfamily. The PtoMBD homodimer has a calculated mass of 42,186 Da.
-	~~My protein is important for saving the world, as can see by the amazing <scene name='93/934002/Ligand/2'>ligand</scene> that is bound to it~~.	+
	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.		This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Isabella Gonzalez at 06:29, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 06:29:08 GMT

←Older revision		Revision as of 06:29, 13 December 2022
Line 7:		Line 7:
	== Function of your protein ==		== Function of your protein ==

-	<scene name='93/934002/Cartoon_image/1'>Mevalonate 3,5-biphosphate decarboxylase</scene> is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the ligand represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined that GGPP or related compounds are possible physiological ligands.	+	<scene name='93/934002/Cartoon_image/1'>Mevalonate 3,5-biphosphate decarboxylase</scene> is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the <scene name='93/934002/Ligand/2'>ligand</scene> represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined that GGPP or related compounds are possible physiological ligands.
	== Biological relevance and broader implications ==		== Biological relevance and broader implications ==

	''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.		''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.
	== Important amino acids==		== Important amino acids==
-	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.	+	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.<scene name='93/934002/Ligand/2'>ligand</scene>
	== Structural highlights ==		== Structural highlights ==
	Secondary Structure		Secondary Structure

Isabella Gonzalez at 06:23, 13 December 2022

Isabella Gonzalez — Tue, 13 Dec 2022 06:23:45 GMT

←Older revision		Revision as of 06:23, 13 December 2022
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	== Function of your protein ==		== Function of your protein ==

-	<scene name='93/934002/Cartoon_image/1'>Mevalonate 3,5-biphosphate decarboxylase</scene> is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the ~~ATP-dependent phosphorylation~~ of the 3-~~hydroxy~~ group of ~~substrates~~. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the ligand represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined that GGPP or related compounds are possible physiological ligands.	+	<scene name='93/934002/Cartoon_image/1'>Mevalonate 3,5-biphosphate decarboxylase</scene> is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the ligand represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined that GGPP or related compounds are possible physiological ligands.
	== Biological relevance and broader implications ==		== Biological relevance and broader implications ==

-	~~The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate.~~''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.	+	''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability.
	== Important amino acids==		== Important amino acids==
	The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.		The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.