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==Structural Basis for Glutamate Racemase Inhibitor== | ==Structural Basis for Glutamate Racemase Inhibitor== | ||
<StructureSection load='2oho' size='340' side='right' caption='[[2oho]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2oho' size='340' side='right'caption='[[2oho]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2oho]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2oho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_(serotype_1_/_m1_gas) Streptococcus pyogenes (serotype 1 / m1 gas)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OHO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b73|1b73]], [[1zuw|1zuw]], [[2ohg|2ohg]], [[2ohv|2ohv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b73|1b73]], [[1zuw|1zuw]], [[2ohg|2ohg]], [[2ohv|2ohv]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">murI ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">murI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=160490 Streptococcus pyogenes (serotype 1 / M1 GAS)])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate_racemase Glutamate racemase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oho OCA], [https://pdbe.org/2oho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oho RCSB], [https://www.ebi.ac.uk/pdbsum/2oho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oho ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MURI_STRP1 MURI_STRP1]] 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]] | ||
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==See Also== | ==See Also== | ||
*[[Glutamate racemase|Glutamate racemase]] | *[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 39: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glutamate racemase]] | [[Category: Glutamate racemase]] | ||
[[Category: Large Structures]] | |||
[[Category: Kim, E E]] | [[Category: Kim, E E]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Racemase]] | [[Category: Racemase]] | ||
Revision as of 15:56, 9 June 2021
Structural Basis for Glutamate Racemase InhibitorStructural Basis for Glutamate Racemase Inhibitor
Structural highlights
Function[MURI_STRP1] 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 PubMedD-Glutamic acid is a required biosynthetic building block for peptidoglycan, and the enzyme glutamate racemase (GluR) catalyzes the inter-conversion of D and L-glutamate enantiomers. Therefore, GluR is considered as an attractive target for the design of new antibacterial drugs. Here, we report the crystal structures of GluR from Streptococcus pyogenes in both inhibitor-free and inhibitor-bound forms. The inhibitor free GluR crystallized in two different forms, which diffracted to 2.25 A and 2.5 A resolution, while the inhibitor-bound crystal diffracted to 2.5 A resolution. GluR is composed of two domains of alpha/beta protein that are related by pseudo-2-fold symmetry and the active site is located at the domain interface. The inhibitor, gamma-2-naphthylmethyl-D-glutamate, which was reported earlier as a novel potent competitive inhibitor, makes several hydrogen bonds with protein atoms, and the naphthyl moiety is located in the hydrophobic pocket. The inhibitor binding induces a disorder in one of the loops near the active site. In both crystal forms, GluR exists as a dimer and the interactions seen at the dimer interface are almost identical. This agrees well with the results from gel filtration and dynamic light-scattering studies. Structural basis for glutamate racemase inhibition.,Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE J Mol Biol. 2007 Sep 14;372(2):434-43. Epub 2007 May 10. PMID:17658548[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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