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''' | + | {{Structure |
| + | |PDB= 1pg4 |SIZE=350|CAPTION= <scene name='initialview01'>1pg4</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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] | ||
| + | |GENE= ACS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28901 Salmonella enterica]) | ||
| + | }} | ||
| + | |||
| + | '''Acetyl CoA Synthetase, Salmonella enterica''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PG4 is a [ | + | 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 1NNM. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12627952 12627952] |
[[Category: Acetate--CoA ligase]] | [[Category: Acetate--CoA ligase]] | ||
[[Category: Salmonella enterica]] | [[Category: Salmonella enterica]] | ||
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[[Category: amp-forming; adenylate-forming; thioester-forming]] | [[Category: amp-forming; adenylate-forming; thioester-forming]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:54 2008'' |
Revision as of 11:23, 20 March 2008
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| , resolution 1.75Å | |||||||
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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, 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
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