1pg4: Difference between revisions
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|PDB= 1pg4 |SIZE=350|CAPTION= <scene name='initialview01'>1pg4</scene>, resolution 1.75Å | |PDB= 1pg4 |SIZE=350|CAPTION= <scene name='initialview01'>1pg4</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRX:ADENOSINE-5'-MONOPHOSPHATE-PROPYL+ESTER'>PRX</scene> | ||
|ACTIVITY= <span class='plainlinks'>[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] </span> | |||
|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]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1pg3|1PG3]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pg4 OCA], [http://www.ebi.ac.uk/pdbsum/1pg4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pg4 RCSB]</span> | |||
}} | }} | ||
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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 Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:10 2008'' | ||
Revision as of 22:59, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | ACS (Salmonella enterica) | ||||||
| Activity: | Acetate--CoA ligase, with EC number 6.2.1.1 | ||||||
| Related: | 1PG3
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Acetyl CoA Synthetase, Salmonella enterica
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
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.
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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