1b73

From Proteopedia

(Difference between revisions)

Revision as of 23:45, 10 September 2015

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

Structural highlights

1b73 is a 1 chain structure with sequence from Aquifex pyrophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1b74
Activity:	Glutamate racemase, with EC number 5.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[MURI_AQUPY] Provides the (R)-glutamate required for cell wall biosynthesis. Converts L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine.

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 (MurI) is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls. The crystal structure of glutamate racemase from Aquifex pyrophilus, determined at 2.3 A resolution, reveals that the enzyme forms a dimer and each monomer consists of two alpha/beta fold domains, a unique structure that has not been observed in other racemases or members of an enolase superfamily. A substrate analog, D-glutamine, binds to the deep pocket formed by conserved residues from two monomers. The structural and mutational analyses allow us to propose a mechanism of metal cofactor-independent glutamate racemase in which two cysteine residues are involved in catalysis.

Structure and mechanism of glutamate racemase from Aquifex pyrophilus.,Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hwang KY, Cho CS, Kim SS, Sung HC, Yu YG, Cho Y. Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat Struct Biol. 1999 May;6(5):422-6. PMID:10331867 doi:10.1038/8223

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b73"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b74|1b74]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b73 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b73 RCSB], [http://www.ebi.ac.uk/pdbsum/1b73 PDBsum]</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=1b73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b73 OCA], [http://pdbe.org/1b73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b73 RCSB], [http://www.ebi.ac.uk/pdbsum/1b73 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1b73" style="background-color:#fffaf0;"></div>
 ==See Also==

1b73

From Proteopedia

Revision as of 23:45, 10 September 2015

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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