2jfo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:37, 9 May 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2jfo.jpg|left|200px]]
 
-
{{Structure
+
==Crystal structure of Enterococcus faecalis glutamate racemase in complex with D- and L-Glutamate==
-
|PDB= 2jfo |SIZE=350|CAPTION= <scene name='initialview01'>2jfo</scene>, resolution 2.5&Aring;
+
<StructureSection load='2jfo' size='340' side='right'caption='[[2jfo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:Dgl+Binding+Site+For+Chain+B'>AC1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene> and <scene name='pdbligand=DGL:D-GLUTAMIC ACID'>DGL</scene>
+
<table><tr><td colspan='2'>[[2jfo]] 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=2JFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JFO FirstGlance]. <br>
-
|ACTIVITY= [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]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-
|GENE=
+
<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>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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=2jfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfo OCA], [https://pdbe.org/2jfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfo RCSB], [https://www.ebi.ac.uk/pdbsum/2jfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfo ProSAT]</span></td></tr>
 +
</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 ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/2jfo_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jfo ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
'''CRYSTAL STRUCTURE OF ENTEROCOCCUS FAECALIS GLUTAMATE RACEMASE IN COMPLEX WITH D- AND L-GLUTAMATE'''
+
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<ref>PMID:17568739</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2jfo" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Glutamate racemase 3D structures|Glutamate racemase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
2JFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFO OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/17568739 17568739]
+
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
-
[[Category: Glutamate racemase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Lundqvist T]]
-
[[Category: Lundqvist, T.]]
+
-
[[Category: DGL]]
+
-
[[Category: GLU]]
+
-
[[Category: glutamate racemase]]
+
-
[[Category: isomerase]]
+
-
[[Category: peptidoglycan biosynthesis]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:41:16 2008''
+

Current revision

Crystal structure of Enterococcus faecalis glutamate racemase in complex with D- and L-Glutamate

PDB ID 2jfo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jfo"
Personal tools