1pg3: Difference between revisions
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'''Acetyl CoA Synthetase, Acetylated on Lys609''' | '''Acetyl CoA Synthetase, Acetylated on Lys609''' | ||
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==About this Structure== | ==About this Structure== | ||
1PG3 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 | 1PG3 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=1nnn 1nnn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG3 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: Lysine acetylation]] | ||
[[Category: | [[Category: Thioester-forming]] | ||
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Revision as of 05:02, 3 May 2008
Acetyl CoA Synthetase, Acetylated on Lys609
OverviewOverview
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 StructureAbout this Structure
1PG3 is a Single protein structure of sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1nnn. Full crystallographic information is available from OCA.
ReferenceReference
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 05:02:54 2008