1pg3: Difference between revisions
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|PDB= 1pg3 |SIZE=350|CAPTION= <scene name='initialview01'>1pg3</scene>, resolution 2.30Å | |PDB= 1pg3 |SIZE=350|CAPTION= <scene name='initialview01'>1pg3</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PRX:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PRX:ADENOSINE-5'-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= [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] | ||
|GENE= ACS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 Salmonella enterica]) | |GENE= ACS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 Salmonella enterica]) | ||
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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://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:12:16 2008'' | ||
Revision as of 14:12, 23 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | , , and | ||||||
| Gene: | ACS (Salmonella enterica) | ||||||
| Activity: | Acetate--CoA ligase, with EC number 6.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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