1pg4
From Proteopedia
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[[Image:1pg4.gif|left|200px]] | [[Image:1pg4.gif|left|200px]] | ||
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'''Acetyl CoA Synthetase, Salmonella enterica''' | '''Acetyl CoA Synthetase, Salmonella enterica''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PG4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. This structure supersedes the now removed PDB entry | + | 1PG4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nnm 1nnm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Horswill, A R.]] | [[Category: Horswill, A R.]] | ||
[[Category: Starai, V J.]] | [[Category: Starai, V J.]] | ||
| - | [[Category: | + | [[Category: Adenylate-forming]] |
| - | [[Category: | + | [[Category: Amp-forming]] |
| - | [[Category: | + | [[Category: Thioester-forming]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:02:59 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 02:03, 3 May 2008
Acetyl CoA Synthetase, Salmonella enterica
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
1PG4 is a Single protein structure of sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1nnm. 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 Page seeded by OCA on Sat May 3 05:02:59 2008
