4esx: Difference between revisions
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New page: '''Unreleased structure''' The entry 4esx is ON HOLD Authors: Huang, S., Fenwick, M.K., Zhang, Y., Lai, R., Hazra, A., Rajashankar, K, Philmus, B., Kinsland, C., Sanders, J., Begley, T.... |
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==Crystal structure of C. albicans Thi5 complexed with PLP== | |||
<StructureSection load='4esx' size='340' side='right'caption='[[4esx]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== Function == | |||
[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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Candida albicans WO-1]] | |||
[[Category: Large Structures]] | |||
[[Category: Begley TP]] | |||
[[Category: Ealick SE]] | |||
[[Category: Fenwick MK]] | |||
[[Category: Hazra A]] | |||
[[Category: Huang S]] | |||
[[Category: Kinsland C]] | |||
[[Category: Lai R]] | |||
[[Category: Philmus B]] | |||
[[Category: Rajashankar K]] | |||
[[Category: Sanders J]] | |||
[[Category: Zhang Y]] | |||
Latest revision as of 06:47, 3 April 2024
Crystal structure of C. albicans Thi5 complexed with PLP
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