5nw7: Difference between revisions
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<StructureSection load='5nw7' size='340' side='right' caption='[[5nw7]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='5nw7' size='340' side='right' caption='[[5nw7]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nw7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NW7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5nw7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NW7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9C2:[(2~{R},3~{R},4~{S})-5-diazanyl-2,3,4-tris(oxidanyl)-5-oxidanylidene-pentyl]+dihydrogen+phosphate'>9C2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9C2:[(2~{R},3~{R},4~{S})-5-diazanyl-2,3,4-tris(oxidanyl)-5-oxidanylidene-pentyl]+dihydrogen+phosphate'>9C2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMI1, MANA, CAALFM_C209640WA, CaO19.1390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Candida stellatoidea]]])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-6-phosphate_isomerase Mannose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.8 5.3.1.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-6-phosphate_isomerase Mannose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.8 5.3.1.8] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nw7 OCA], [http://pdbe.org/5nw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5nw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nw7 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nw7 OCA], [http://pdbe.org/5nw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nw7 RCSB], [http://www.ebi.ac.uk/pdbsum/5nw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nw7 ProSAT]</span></td></tr> | ||
Revision as of 11:01, 14 June 2018
Crystal structure of candida albicans phosphomannose isomerase in complex with inhibitorCrystal structure of candida albicans phosphomannose isomerase in complex with inhibitor
Structural highlights
Function[MPI_CANAL] Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. Publication Abstract from PubMedType I phosphomannose isomerases (PMIs) are zinc-dependent monofunctional metalloenzymes catalyzing the reversible isomerization of d-mannose 6-phosphate to d-fructose 6-phosphate. 5-Phospho-d-arabinonhydrazide (5PAHz), designed as an analogue of the enediolate high-energy intermediate, strongly inhibits PMI from Candida albicans (CaPMI). In this study, we report the 3D crystal structure of CaPMI complexed with 5PAHz at 1.85 A resolution. The high-resolution structure suggests that Glu294 is the catalytic base that transfers a proton between the C1 and C2 carbon atoms of the substrate. Bidentate coordination of the inhibitor explains the stereochemistry of the isomerase activity, as well as the absence of both anomerase and C2-epimerase activities for Type I PMIs. A detailed mechanism of the reversible isomerization is proposed. This article is protected by copyright. All rights reserved. Crystal Structure of Phosphomannose Isomerase from Candida albicans Complexed with 5-Phospho-d-Arabinonhydrazide.,Ahmad L, Plancqueel S, Dubosclard V, Lazar N, Ghattas W, Li de la Sierra-Gallay I, van Tilbeurgh H, Salmon L FEBS Lett. 2018 Apr 23. doi: 10.1002/1873-3468.13059. PMID:29687459[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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