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4esx

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'''Unreleased structure'''
 
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The entry 4esx is ON HOLD
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==Crystal structure of C. albicans Thi5 complexed with PLP==
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<StructureSection load='4esx' size='340' side='right'caption='[[4esx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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Authors: Huang, S., Fenwick, M.K., Zhang, Y., Lai, R., Hazra, A., Rajashankar, K, Philmus, B., Kinsland, C., Sanders, J., Begley, T.P., Ealick, S.E.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4esx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_WO-1 Candida albicans WO-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ESX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ESX FirstGlance]. <br>
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Description: Crystal structure of C. albicans Thi5 complexed with PLP
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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]] 2.2&#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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=4esx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4esx OCA], [https://pdbe.org/4esx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4esx RCSB], [https://www.ebi.ac.uk/pdbsum/4esx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4esx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THI5_CANAW THI5_CANAW] Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.<ref>PMID:22568620</ref>
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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: Candida albicans WO-1]]
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[[Category: Large Structures]]
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[[Category: Begley TP]]
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[[Category: Ealick SE]]
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[[Category: Fenwick MK]]
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[[Category: Hazra A]]
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[[Category: Huang S]]
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[[Category: Kinsland C]]
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[[Category: Lai R]]
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[[Category: Philmus B]]
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[[Category: Rajashankar K]]
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[[Category: Sanders J]]
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[[Category: Zhang Y]]

Current revision

Crystal structure of C. albicans Thi5 complexed with PLP

PDB ID 4esx

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