1b74
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene> | |LIGAND= <scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene> | ||
| - | |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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1b73|1B73]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b74 OCA], [http://www.ebi.ac.uk/pdbsum/1b74 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b74 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kim, S S.]] | [[Category: Kim, S S.]] | ||
[[Category: Yu, Y G.]] | [[Category: Yu, Y G.]] | ||
| - | [[Category: DGN]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
[[Category: racemase]] | [[Category: racemase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:07 2008'' |
Revision as of 15:55, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Glutamate racemase, with EC number 5.1.1.3 | ||||||
| Related: | 1B73
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS
Overview
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.
About this Structure
1B74 is a Single protein structure of sequence from Aquifex pyrophilus. Full crystallographic information is available from OCA.
Reference
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
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