|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of Enterococcus faecalis glutamate racemase in complex with D- Glutamate== | | ==Crystal structure of Enterococcus faecalis glutamate racemase in complex with D- Glutamate== |
| - | <StructureSection load='2jfp' size='340' side='right' caption='[[2jfp]], [[Resolution|resolution]] 1.98Å' scene=''> | + | <StructureSection load='2jfp' size='340' side='right'caption='[[2jfp]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jfp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JFP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jfp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JFP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jfn|2jfn]], [[2jfo|2jfo]], [[2jfq|2jfq]], [[2jfu|2jfu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.3 5.1.1.3] </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=2jfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfp OCA], [https://pdbe.org/2jfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfp RCSB], [https://www.ebi.ac.uk/pdbsum/2jfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfp 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=2jfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfp OCA], [http://pdbe.org/2jfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jfp RCSB], [http://www.ebi.ac.uk/pdbsum/2jfp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfp ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MURI_ENTFA MURI_ENTFA] Provides the (R)-glutamate required for cell wall biosynthesis.[HAMAP-Rule:MF_00258] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 28: |
Line 29: |
| | </div> | | </div> |
| | <div class="pdbe-citations 2jfp" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2jfp" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| - | [[Category: Glutamate racemase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lundqvist, T]] | + | [[Category: Lundqvist T]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Peptidoglycan biosynthesis]]
| + | |
| Structural highlights
Function
MURI_ENTFA Provides the (R)-glutamate required for cell wall biosynthesis.[HAMAP-Rule:MF_00258]
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 PubMed
Glutamate 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 Also
References
- ↑ Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL. Exploitation of structural and regulatory diversity in glutamate racemases. Nature. 2007 Jun 14;447(7146):817-22. PMID:17568739 doi:http://dx.doi.org/10.1038/nature05689
|
