1ry2

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(New page: 200px<br /><applet load="1ry2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ry2, resolution 2.30&Aring;" /> '''Crystal structure of...)
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[[Image:1ry2.jpg|left|200px]]<br /><applet load="1ry2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ry2, resolution 2.30&Aring;" />
 
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'''Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP'''<br />
 
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==Overview==
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==Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP==
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Acetyl-coenzyme A synthetase (ACS) belongs to the family of AMP-forming, enzymes that also includes acyl-CoA synthetases, firefly luciferase, and, nonribosomal peptide synthetases. ACS catalyzes the two-step activation of, acetate to acetyl-CoA: formation of an acetyl-AMP intermediate from, acetate and ATP and the transfer of the acetyl group to CoA. In mammals, the acetyl-CoA product is used for biosynthesis of long chain fatty acids, as well as energy production. We have determined the crystal structure of, yeast ACS in a binary complex with AMP at 2.3 A resolution. The structure, contains a large, N-terminal domain and a small, C-terminal domain. AMP is, bound at the interface between the two domains. This structure represents, a new conformation for the ACS enzyme, which may be competent for, catalyzing the first step of the reaction. A Lys residue that is critical, for this step is located in the active site. A rotation of 140 degrees in, the small domain is needed for the binding of CoA and the catalysis of the, second step. In contrast to the monomeric bacterial enzyme, yeast ACS is a, stable trimer.
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<StructureSection load='1ry2' size='340' side='right'caption='[[1ry2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ry2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RY2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ry2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry2 OCA], [https://pdbe.org/1ry2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ry2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ry2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ry2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACS1_YEAST ACS1_YEAST] Catalyzes the production of acetyl-CoA. Provides the acetyl-CoA source for histone acetylation in the nucleus. "Aerobic" isozyme of acetyl-coenzyme A synthetase, which supports growth on nonfermentable carbon sources such as glycerol and ethanol. May be required for assimilation of ethanol and acetate.<ref>PMID:8910545</ref> <ref>PMID:16857587</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ry/1ry2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ry2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acetyl-coenzyme A synthetase (ACS) belongs to the family of AMP-forming enzymes that also includes acyl-CoA synthetases, firefly luciferase, and nonribosomal peptide synthetases. ACS catalyzes the two-step activation of acetate to acetyl-CoA: formation of an acetyl-AMP intermediate from acetate and ATP and the transfer of the acetyl group to CoA. In mammals, the acetyl-CoA product is used for biosynthesis of long chain fatty acids as well as energy production. We have determined the crystal structure of yeast ACS in a binary complex with AMP at 2.3 A resolution. The structure contains a large, N-terminal domain and a small, C-terminal domain. AMP is bound at the interface between the two domains. This structure represents a new conformation for the ACS enzyme, which may be competent for catalyzing the first step of the reaction. A Lys residue that is critical for this step is located in the active site. A rotation of 140 degrees in the small domain is needed for the binding of CoA and the catalysis of the second step. In contrast to the monomeric bacterial enzyme, yeast ACS is a stable trimer.
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==About this Structure==
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Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP.,Jogl G, Tong L Biochemistry. 2004 Feb 17;43(6):1425-31. PMID:14769018<ref>PMID:14769018</ref>
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1RY2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with AMP as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1RY2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP., Jogl G, Tong L, Biochemistry. 2004 Feb 17;43(6):1425-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14769018 14769018]
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</div>
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[[Category: Acetate--CoA ligase]]
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<div class="pdbe-citations 1ry2" style="background-color:#fffaf0;"></div>
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Jogl, G.]]
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[[Category: Tong, L.]]
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[[Category: AMP]]
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[[Category: amp forming; related to firefly luciferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:56:55 2007''
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==See Also==
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*[[Acetyl-CoA synthetase 3D structures|Acetyl-CoA synthetase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Jogl G]]
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[[Category: Tong L]]

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Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

PDB ID 1ry2

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