2vze

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{{Seed}}
 
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[[Image:2vze.png|left|200px]]
 
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==Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in complex with AMP==
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The line below this paragraph, containing "STRUCTURE_2vze", creates the "Structure Box" on the page.
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<StructureSection load='2vze' size='340' side='right'caption='[[2vze]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vze]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.45&#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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2vze| PDB=2vze | SCENE= }}
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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=2vze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vze OCA], [https://pdbe.org/2vze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vze RCSB], [https://www.ebi.ac.uk/pdbsum/2vze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vze ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACS2A_HUMAN ACS2A_HUMAN] Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity).
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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/vz/2vze_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=2vze 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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Acyl-CoA synthetases belong to the superfamily of adenylate-forming enzymes, and catalyze the two-step activation of fatty acids or carboxylate-containing xenobiotics. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Here, we report the first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/product/cofactor complexes central to the catalytic mechanism. We observed a substantial rearrangement between the N- and C-terminal domains, driven purely by the identity of the bound ligand in the active site. Our structures allowed us to identify the presence or absence of the ATP pyrophosphates as the conformational switch, and elucidated new mechanistic details, including the role of invariant Lys557 and a divalent magnesium ion in coordinating the ATP pyrophosphates, as well as the involvement of a Gly-rich P-loop and the conserved Arg472-Glu365 salt bridge in the domain rearrangement.
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===CRYSTAL STRUCTURE OF HUMAN ACYL-COA SYNTHETASE MEDIUM-CHAIN FAMILY MEMBER 2A (L64P MUTATION) IN COMPLEX WITH AMP===
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Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.,Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. PMID:19345228<ref>PMID:19345228</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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2VZE is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZE OCA].
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<div class="pdbe-citations 2vze" style="background-color:#fffaf0;"></div>
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[[Category: Butyrate--CoA ligase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Large Structures]]
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[[Category: Bhatia, C.]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C.]]
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[[Category: Bhatia C]]
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[[Category: Delft, F Von.]]
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[[Category: Bountra C]]
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[[Category: Edwards, A M.]]
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[[Category: Edwards AM]]
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[[Category: Kochan, G T.]]
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[[Category: Kochan GT]]
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[[Category: Oppermann, U.]]
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[[Category: Oppermann U]]
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[[Category: Pilka, E S.]]
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[[Category: Pilka ES]]
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[[Category: Wikstrom, M.]]
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[[Category: Wikstrom M]]
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[[Category: Yue, W W.]]
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[[Category: Yue WW]]
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[[Category: Adenylate-forming enzyme]]
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[[Category: Von Delft F]]
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[[Category: Atp-binding]]
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[[Category: Fatty acid metabolism]]
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[[Category: Fatty acid-coa ligase]]
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[[Category: Ligase]]
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[[Category: Lipid metabolism]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Mitochondrion]]
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[[Category: Nucleotide-binding]]
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[[Category: Polymorphism]]
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[[Category: Transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:17:47 2009''
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Current revision

Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in complex with AMP

PDB ID 2vze

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OCA

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