1b74

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{{STRUCTURE_1b74| PDB=1b74 | SCENE= }}
{{STRUCTURE_1b74| PDB=1b74 | SCENE= }}
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'''GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS'''
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===GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10331867 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10331867}}
==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Racemase]]
[[Category: Racemase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:25:35 2008''

Revision as of 15:25, 30 June 2008

Image:1b74.png

Template:STRUCTURE 1b74

GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS

Template:ABSTRACT PUBMED 10331867

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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