5a0z

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'''Unreleased structure'''
 
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The entry 5a0z is ON HOLD until Paper Publication
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==STRUCTURE OF CUTC CHOLINE LYASE CHOLINE FREE FORM FROM KLEBSIELLA PNEUMONIAE==
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<StructureSection load='5a0z' size='340' side='right'caption='[[5a0z]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5a0z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0Z 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]] 3&#8491;</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=5a0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0z OCA], [https://pdbe.org/5a0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0z RCSB], [https://www.ebi.ac.uk/pdbsum/5a0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0M3KL45_KLEPN A0A0M3KL45_KLEPN] Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde.[HAMAP-Rule:MF_02058]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CutC choline trimethylamine lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the gut microbiota, and its metabolite, trimethylamine oxide (TMAO), has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-bound and the choline-free forms of CutC and have discovered that binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure, a feature that has not been observed for any other characterized GRE.
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Authors: Kalnins, G., Tars, K.
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Structure and function of CutC choline lyase from human microbiota bacterium Klebsiella pneumoniae.,Kalnins G, Kuka J, Grinberga S, Makrecka-Kuka M, Liepinsh E, Dambrova M, Tars K J Biol Chem. 2015 Jul 17. pii: jbc.M115.670471. PMID:26187464<ref>PMID:26187464</ref>
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Description: STRUCTURE OF CUTC CHOLINE LYASE CHOLINE FREE FORM FROM KLEBSIELLA PNEUMONIAE
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Tars, K]]
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<div class="pdbe-citations 5a0z" style="background-color:#fffaf0;"></div>
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[[Category: Kalnins, G]]
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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: Klebsiella pneumoniae]]
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[[Category: Large Structures]]
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[[Category: Kalnins G]]
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[[Category: Tars K]]

Current revision

STRUCTURE OF CUTC CHOLINE LYASE CHOLINE FREE FORM FROM KLEBSIELLA PNEUMONIAE

PDB ID 5a0z

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