6mnv
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of X. citri phosphoglucomutase in complex with CH2FG1P== | |
| + | <StructureSection load='6mnv' size='340' side='right'caption='[[6mnv]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mnv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MNV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MNV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JVS:1-deoxy-1-fluoro-2-O-phosphono-alpha-D-gluco-hept-2-ulopyranose'>JVS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mlf|6mlf]], [[6mlh|6mlh]], [[6mlw|6mlw]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] </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=6mnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mnv OCA], [http://pdbe.org/6mnv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mnv RCSB], [http://www.ebi.ac.uk/pdbsum/6mnv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mnv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | alpha-Phosphomannomutase/phosphoglucomutase (alphaPMM/PGM) from P. aeruginosa is involved in bacterial cell wall assembly and is implicated in P. aeruginosa virulence, yet few studies have addressed alphaPMM/PGM inhibition from this important Gram-negative bacterial human pathogen. Four structurally different alpha-d-glucopyranose 1-phosphate (alphaG1P) derivatives including 1-C-fluoromethylated analogues (1-3), 1,2-cyclic phosph(on)ate analogues (4-6), isosteric methylene phosphono analogues (7 and 8), and 6-fluoro-alphaG1P (9), were synthesized and assessed as potential time-dependent or reversible alphaPMM/PGM inhibitors. The resulting kinetic data were consistent with the crystallographic structures of the highly homologous Xanthomonas citri alphaPGM with inhibitors 3 and 7-9 binding to the enzyme active site (1.65-1.9 A). These structural and kinetic insights will enhance the design of future alphaPMM/PGM inhibitors. | ||
| - | + | Inhibitory Evaluation of alphaPMM/PGM from Pseudomonas aeruginosa: Chemical Synthesis, Enzyme Kinetics, and Protein Crystallographic Study.,Zhu JS, Stiers KM, Soleimani E, Groves BR, Beamer LJ, Jakeman DL J Org Chem. 2019 Jul 16. doi: 10.1021/acs.joc.9b01305. PMID:31264865<ref>PMID:31264865</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6mnv" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phosphoglucomutase]] | ||
[[Category: Beamer, L]] | [[Category: Beamer, L]] | ||
| + | [[Category: Stiers, K]] | ||
| + | [[Category: Carbohydrate biosynthesis]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Isomerase]] | ||
Revision as of 06:20, 31 July 2019
Crystal structure of X. citri phosphoglucomutase in complex with CH2FG1P
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