Glutamate racemase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:51, 11 July 2019) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='2jfq' size='350' side='right' caption='Structure of glutamate racemase dimer complex with D-glutamate (PDB entry [[2jfq]])' scene=''>
+
<StructureSection load='2jfz' size='350' side='right' caption='Structure of glutamate racemase dimer complex with D-glutamate and inhibitor (PDB entry [[2jfz]])' scene='55/551210/Cv/1'>
 +
== Function ==
-
'''Glutamate racemase''' (GR) catalyzes the racemization of L-glutamate to D-glutamate. GR plays a major role in bacterial cell wall biosynthesis and moonlights as gyrase inhibitor. GR inhibition is used as anti-bacterial target.
+
'''Glutamate racemase''' (GR) catalyzes the racemization of L-glutamate to D-glutamate. GR plays a major role in bacterial cell wall biosynthesis and moonlights as gyrase inhibitor<ref>PMID:18757813</ref>.
-
</StructureSection>
+
-
== 3D Structures of glutamate racemase ==
+
== Relevance ==
 +
GR inhibition is used as anti-bacterial target<ref>PMID:22877632</ref>.
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
== Structural highlights ==
-
{{#tree:id=OrganizedByTopic|openlevels=0|
+
The <scene name='55/551210/Cv/6'>binding site of D-glutamate to GR</scene> is different from that of the <scene name='55/551210/Cv/7'>inhibitor binding site</scene>. Water molecules shown as red spheres. The latter site is occupied in the native GR by side chains of the enzyme<ref>PMID:17568739</ref>
-
*Glutamate racemate
+
== 3D Structures of glutamate racemase ==
 +
[[Glutamate racemase 3D structures]]
-
**[[1b73]], [[1b74]] – GR – ''Aquifex pyrophilus'' <BR />
+
</StructureSection>
-
**[[2gzm]], [[2dwu]] – GR – ''Bacillus anthracis'' <BR />
+
-
**[[2ohg]], [[2oho]] – SpGR – ''Streptococcus pyogenes'' <BR />
+
-
**[[3hfr]] – LmGR – ''Listeria monocytogenes'' <BR />
+
-
**[[3uhp]] – CjGR – ''Campylobacter jejuni'' <BR />
+
-
 
+
-
*Glutamate racemate complexes
+
-
**[[2jfn]] – GR + UDP-acetylmuramoyl-alanine + glutamate – ''Escherichia coli '' <BR />
+
== References ==
-
**[[2jfo]], [[2jfp]] – EfGR + D-glutamate – ''Enterococcus faecalis'' <BR />
+
<references/>
-
**[[2jfq]] – GR + D-glutamate – ''Staphylococcus aureus'' <BR />
+
-
**[[3out]] – GR + D-glutamate – ''Francisella tularensis'' <BR />
+
-
**[[1zuw]] – GR + D-glutamate – ''Bacillus subtilis'' <BR />
+
-
**[[3uhf]], [[3uho]] – CjGR + D-glutamate <BR />
+
-
**[[2jfu]] – EfGR + phosphate <BR />
+
-
**[[2jfv]] – EfGR + citrate <BR />
+
-
**[[2jfw]] – EfGR + tartrate <BR />
+
-
**[[2vvt]] – EfGR + inhibitor <BR />
+
-
**[[3ist]] – LmGR + succinate <BR />
+
-
**[[3isv]] – LmGR + acetate <BR />
+
-
**[[2jfx]], [[2jfy]] – HpGR + D-glutamate – ''Helicobacter pylori '' <BR />
+
-
**[[2jfz]], [[2w4i]], [[4b1f]] – HpGR + D-glutamate + inhibitor <BR />
+
-
**[[2ohv]] – SpGR + D-glutamate derivative inhibitor <BR />
+
-
}}
+
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of glutamate racemase dimer complex with D-glutamate and inhibitor (PDB entry 2jfz)

Drag the structure with the mouse to rotate

References

  1. ↑ Sengupta S, Ghosh S, Nagaraja V. Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme. Microbiology. 2008 Sep;154(Pt 9):2796-803. doi: 10.1099/mic.0.2008/020933-0. PMID:18757813 doi:http://dx.doi.org/10.1099/mic.0.2008/020933-0
  2. ↑ Basarab GS, Hill P, Eyermann CJ, Gowravaram M, Kack H, Osimoni E. Design of inhibitors of Helicobacter pylori glutamate racemase as selective antibacterial agents: Incorporation of imidazoles onto a core pyrazolopyrimidinedione scaffold to improve bioavailabilty. Bioorg Med Chem Lett. 2012 Sep 1;22(17):5600-7. Epub 2012 Jul 20. PMID:22877632 doi:http://dx.doi.org/10.1016/j.bmcl.2012.07.004
  3. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Glutamate_racemase"
Personal tools