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3qdq

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Current revision (11:41, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3qdq' size='340' side='right'caption='[[3qdq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3qdq' size='340' side='right'caption='[[3qdq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qdq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_aminobutyricum"_hardman_and_stadtman "clostridium aminobutyricum" hardman and stadtman]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qdq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_aminobutyricum Clostridium aminobutyricum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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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]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gk7|3gk7]]</div></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=COA:COENZYME+A'>COA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abfT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33953 "Clostridium aminobutyricum" Hardman and Stadtman])</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=3qdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdq OCA], [https://pdbe.org/3qdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdq RCSB], [https://www.ebi.ac.uk/pdbsum/3qdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdq ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdq OCA], [https://pdbe.org/3qdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdq RCSB], [https://www.ebi.ac.uk/pdbsum/3qdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9RM86_CLOAM Q9RM86_CLOAM]
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Clostridium aminobutyricum ferments 4-aminobutyrate (gamma-aminobutyrate, GABA) to ammonia, acetate and butyrate via 4-hydroxybutyrate that is activated to the CoA-thioester catalyzed by 4-hydroxybutyrate CoA-transferase. Then, 4-hydroxybutyryl-CoA is dehydrated to crotonyl-CoA, which disproportionates to butyryl-CoA and acetyl-CoA. Cocrystallization of the CoA-transferase with the alternate substrate butyryl-CoA yielded crystals with non-covalently bound CoA and two water molecules at the active site. Most likely, butyryl-CoA reacted with the active site Glu238 to CoA and the mixed anhydride, which slowly hydrolyzed during crystallization. The structure of the CoA is similar but less stretched than that of the CoA-moiety of the covalent enzyme-CoA-thioester in 4-hydroxybutyrate CoA-transferase from Shewanella oneidensis. In contrast to the structures of the apo-enzyme and enzyme-CoA-thioester, the structure described here has a closed conformation, probably caused by a flip of the active site loop (residues 215-219). During turnover, the closed conformation may protect the anhydride intermediate from hydrolysis and CoA from dissociation from the enzyme. Hence, one catalytic cycle changes conformation of the enzyme four times: free enzyme-open conformation, CoA+ anhydride 1-closed, enzyme-CoA-thioester-open, CoA + anhydride-2-closed, free enzyme-open.
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Crystal structure of the complex between 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum and CoA.,Macieira S, Zhang J, Buckel W, Messerschmidt A Arch Microbiol. 2011 Aug 11. PMID:21833509<ref>PMID:21833509</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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</div>
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<div class="pdbe-citations 3qdq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Clostridium aminobutyricum hardman and stadtman]]
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[[Category: Clostridium aminobutyricum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Macieira, S]]
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[[Category: Macieira S]]
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[[Category: Messerschmidt, A]]
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[[Category: Messerschmidt A]]
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[[Category: Coa]]
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[[Category: Coa transferase family i]]
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[[Category: Single subunit coa transferase]]
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[[Category: Transferase]]
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Current revision

Complex between 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum and CoA

PDB ID 3qdq

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