5nw7: Difference between revisions
New page: '''Unreleased structure''' The entry 5nw7 is ON HOLD until Paper Publication Authors: Li de la Sierra-Gallay, I., Ahmad, L., Plancqueel, S., van Tilbeurgh, H., Salmon, L. Description: ... |
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==Crystal structure of candida albicans phosphomannose isomerase in complex with inhibitor== | |||
<StructureSection load='5nw7' size='340' side='right'caption='[[5nw7]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5nw7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5NW7 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]] 1.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nw7 OCA], [https://pdbe.org/5nw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nw7 RCSB], [https://www.ebi.ac.uk/pdbsum/5nw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nw7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MPI_CANAL MPI_CANAL] Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type 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<ref>PMID:29687459</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5nw7" style="background-color:#fffaf0;"></div> | ||
[[Category: Ahmad | == References == | ||
[[Category: Li | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Candida albicans]] | |||
[[Category: Large Structures]] | |||
[[Category: Ahmad L]] | |||
[[Category: Li de la Sierra-Gallay I]] | |||
[[Category: Plancqueel S]] | |||
[[Category: Salmon L]] | |||
[[Category: Van Tilbeurgh H]] | |||
Latest revision as of 13:54, 17 January 2024
Crystal structure of candida albicans phosphomannose isomerase in complex with inhibitorCrystal structure of candida albicans phosphomannose isomerase in complex with inhibitor
Structural highlights
FunctionMPI_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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