1pg3
From Proteopedia
(New page: 200px<br /><applet load="1pg3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pg3, resolution 2.30Å" /> '''Acetyl CoA Synthetas...) |
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| - | [[Image:1pg3.jpg|left|200px]]<br /><applet load="1pg3" size=" | + | [[Image:1pg3.jpg|left|200px]]<br /><applet load="1pg3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pg3, resolution 2.30Å" /> | caption="1pg3, resolution 2.30Å" /> | ||
'''Acetyl CoA Synthetase, Acetylated on Lys609'''<br /> | '''Acetyl CoA Synthetase, Acetylated on Lys609'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of | + | Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of acetyl-CoA from acetate, ATP, and CoA and belongs to a family of adenylate-forming enzymes that generate an acyl-AMP intermediate. This family includes other acyl- and aryl-CoA synthetases, firefly luciferase, and the adenylation domains of the modular nonribosomal peptide synthetases. We have determined the X-ray crystal structure of acetyl-CoA synthetase complexed with adenosine-5'-propylphosphate and CoA. The structure identifies the CoA binding pocket as well as a new conformation for members of this enzyme family in which the approximately 110-residue C-terminal domain exhibits a large rotation compared to structures of peptide synthetase adenylation domains. This domain movement presents a new set of residues to the active site and removes a conserved lysine residue that was previously shown to be important for catalysis of the adenylation half-reaction. Comparison of our structure with kinetic and structural data of closely related enzymes suggests that the members of the adenylate-forming family of enzymes may adopt two different orientations to catalyze the two half-reactions. Additionally, we provide a structural explanation for the recently shown control of enzyme activity by acetylation of an active site lysine. |
==About this Structure== | ==About this Structure== | ||
| - | 1PG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with MG, COA, PRX and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1PG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=PRX:'>PRX</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1NNN. Active as [http://en.wikipedia.org/wiki/Acetate--CoA_ligase Acetate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.1 6.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella enterica]] | [[Category: Salmonella enterica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Escalante-Semerena, J | + | [[Category: Escalante-Semerena, J C.]] |
| - | [[Category: Gulick, A | + | [[Category: Gulick, A M.]] |
| - | [[Category: Homick, K | + | [[Category: Homick, K M.]] |
| - | [[Category: Horswill, A | + | [[Category: Horswill, A R.]] |
| - | [[Category: Starai, V | + | [[Category: Starai, V J.]] |
[[Category: COA]] | [[Category: COA]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: amp-forming; adenylate-forming; thioester-forming; lysine acetylation]] | [[Category: amp-forming; adenylate-forming; thioester-forming; lysine acetylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:25 2008'' |
Revision as of 12:28, 21 February 2008
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Acetyl CoA Synthetase, Acetylated on Lys609
Overview
Acetyl-coenzyme A synthetase catalyzes the two-step synthesis of acetyl-CoA from acetate, ATP, and CoA and belongs to a family of adenylate-forming enzymes that generate an acyl-AMP intermediate. This family includes other acyl- and aryl-CoA synthetases, firefly luciferase, and the adenylation domains of the modular nonribosomal peptide synthetases. We have determined the X-ray crystal structure of acetyl-CoA synthetase complexed with adenosine-5'-propylphosphate and CoA. The structure identifies the CoA binding pocket as well as a new conformation for members of this enzyme family in which the approximately 110-residue C-terminal domain exhibits a large rotation compared to structures of peptide synthetase adenylation domains. This domain movement presents a new set of residues to the active site and removes a conserved lysine residue that was previously shown to be important for catalysis of the adenylation half-reaction. Comparison of our structure with kinetic and structural data of closely related enzymes suggests that the members of the adenylate-forming family of enzymes may adopt two different orientations to catalyze the two half-reactions. Additionally, we provide a structural explanation for the recently shown control of enzyme activity by acetylation of an active site lysine.
About this Structure
1PG3 is a Single protein structure of sequence from Salmonella enterica with , , and as ligands. This structure supersedes the now removed PDB entry 1NNN. Active as Acetate--CoA ligase, with EC number 6.2.1.1 Full crystallographic information is available from OCA.
Reference
The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A., Gulick AM, Starai VJ, Horswill AR, Homick KM, Escalante-Semerena JC, Biochemistry. 2003 Mar 18;42(10):2866-73. PMID:12627952
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