2jfx: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2jfx' size='340' side='right'caption='[[2jfx]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2jfx' size='340' side='right'caption='[[2jfx]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2jfx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2jfx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JFX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</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=2jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfx OCA], [https://pdbe.org/2jfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfx RCSB], [https://www.ebi.ac.uk/pdbsum/2jfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfx ProSAT]</span></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=2jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfx OCA], [https://pdbe.org/2jfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfx RCSB], [https://www.ebi.ac.uk/pdbsum/2jfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MURI_HELPJ MURI_HELPJ] Provides the (R)-glutamate required for cell wall biosynthesis (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 37: | Line 36: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Helicobacter pylori]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lundqvist | [[Category: Lundqvist T]] | ||
[[Category: Xue | [[Category: Xue Y]] | ||
Latest revision as of 12:37, 9 May 2024
Crystal structure of Helicobacter pylori glutamate racemase in complex with D-GlutamateCrystal structure of Helicobacter pylori glutamate racemase in complex with D-Glutamate
Structural highlights
FunctionMURI_HELPJ Provides the (R)-glutamate required for cell wall biosynthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and has therefore been considered as a target for antibacterial drug discovery. We characterized the glutamate racemases of several pathogenic bacteria using structural and biochemical approaches. Here we describe three distinct mechanisms of regulation for the family of glutamate racemases: allosteric activation by metabolic precursors, kinetic regulation through substrate inhibition, and D-glutamate recycling using a d-amino acid transaminase. In a search for selective inhibitors, we identified a series of uncompetitive inhibitors specifically targeting Helicobacter pylori glutamate racemase that bind to a cryptic allosteric site, and used these inhibitors to probe the mechanistic and dynamic features of the enzyme. These structural, kinetic and mutational studies provide insight into the physiological regulation of these essential enzymes and provide a basis for designing narrow-spectrum antimicrobial agents. Exploitation of structural and regulatory diversity in glutamate racemases.,Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL Nature. 2007 Jun 14;447(7146):817-22. PMID:17568739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||