6n1e: Difference between revisions
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<StructureSection load='6n1e' size='340' side='right'caption='[[6n1e]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6n1e' size='340' side='right'caption='[[6n1e]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6n1e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N1E FirstGlance]. <br> | <table><tr><td colspan='2'>[[6n1e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"xanthomonas_citri"_(hasse_1915)_dowson_1939 "xanthomonas citri" (hasse 1915) dowson 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N1E FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=QIF:1-deoxy-7-O-phosphono-alpha-D-gluco-hept-2-ulopyranose'>QIF</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=QIF:1-deoxy-7-O-phosphono-alpha-D-gluco-hept-2-ulopyranose'>QIF</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xavtCFBP7764_14885 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=346 "Xanthomonas citri" (Hasse 1915) Dowson 1939])</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=6n1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n1e OCA], [http://pdbe.org/6n1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n1e RCSB], [http://www.ebi.ac.uk/pdbsum/6n1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n1e 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=6n1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n1e OCA], [http://pdbe.org/6n1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n1e RCSB], [http://www.ebi.ac.uk/pdbsum/6n1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n1e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glucokinase phosphorylated a series of C-1 fluorinated alpha-d-gluco-heptuloses. These phosphorylated products were discovered to be inhibitors of alpha-phosphomannomutase/phosphoglucomutase (alphaPMM/PGM) and beta-phosphoglucomutase (betaPGM). Inhibition potency with both mutases inversely correlated to the degree of fluorination. Structural analysis with alphaPMM demonstrated the inhibitor binding to the active site, with the phosphate in the phosphate binding site and the anomeric hydroxyl directed to the catalytic site. | |||
Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition.,Zhu JS, Stiers KM, Winter SM, Garcia AD, Versini AF, Beamer LJ, Jakeman DL ACS Omega. 2019 Apr 30;4(4):7029-7037. doi: 10.1021/acsomega.9b00008. Epub 2019, Apr 18. PMID:31179410<ref>PMID:31179410</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6n1e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 14:40, 13 November 2019
Crystal structure of X. citri phosphoglucomutase in complex with 1-methyl-glucose 6-phosphateCrystal structure of X. citri phosphoglucomutase in complex with 1-methyl-glucose 6-phosphate
Structural highlights
Publication Abstract from PubMedGlucokinase phosphorylated a series of C-1 fluorinated alpha-d-gluco-heptuloses. These phosphorylated products were discovered to be inhibitors of alpha-phosphomannomutase/phosphoglucomutase (alphaPMM/PGM) and beta-phosphoglucomutase (betaPGM). Inhibition potency with both mutases inversely correlated to the degree of fluorination. Structural analysis with alphaPMM demonstrated the inhibitor binding to the active site, with the phosphate in the phosphate binding site and the anomeric hydroxyl directed to the catalytic site. Synthesis, Derivatization, and Structural Analysis of Phosphorylated Mono-, Di-, and Trifluorinated d-Gluco-heptuloses by Glucokinase: Tunable Phosphoglucomutase Inhibition.,Zhu JS, Stiers KM, Winter SM, Garcia AD, Versini AF, Beamer LJ, Jakeman DL ACS Omega. 2019 Apr 30;4(4):7029-7037. doi: 10.1021/acsomega.9b00008. Epub 2019, Apr 18. PMID:31179410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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