1pg3: Difference between revisions

Revision as of 23:00, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pg3.png

Template:STRUCTURE 1pg3

Acetyl CoA Synthetase, Acetylated on Lys609Acetyl CoA Synthetase, Acetylated on Lys609

Template:ABSTRACT PUBMED 12627952

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

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OCA

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-'''Acetyl CoA Synthetase, Acetylated on Lys609'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12627952}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Lysine acetylation]]
 [[Category: Thioester-forming]]
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