1pg4: Difference between revisions

New page: left|200px<br /><applet load="1pg4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pg4, resolution 1.75Å" /> '''Acetyl CoA Synthetas...
 
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'''Acetyl CoA Synthetase, Salmonella enterica'''<br />
'''Acetyl CoA Synthetase, Salmonella enterica'''<br />


==Overview==
==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.
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==
==About this Structure==
1PG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with CL, MG, COA, PRX and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1NNM. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA].  
1PG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=PRX:'>PRX</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1NNM. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PG4 OCA].  


==Reference==
==Reference==
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[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Escalante-Semerena, J.C.]]
[[Category: Escalante-Semerena, J C.]]
[[Category: Gulick, A.M.]]
[[Category: Gulick, A M.]]
[[Category: Homick, K.M.]]
[[Category: Homick, K M.]]
[[Category: Horswill, A.R.]]
[[Category: Horswill, A R.]]
[[Category: Starai, V.J.]]
[[Category: Starai, V J.]]
[[Category: CL]]
[[Category: CL]]
[[Category: COA]]
[[Category: COA]]
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[[Category: amp-forming; adenylate-forming; thioester-forming]]
[[Category: amp-forming; adenylate-forming; thioester-forming]]


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