1b73: Difference between revisions

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[[Image:1b73.jpg|left|200px]]
{{Seed}}
[[Image:1b73.png|left|200px]]


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{{STRUCTURE_1b73|  PDB=1b73  |  SCENE=  }}  
{{STRUCTURE_1b73|  PDB=1b73  |  SCENE=  }}  


'''GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS'''
===GLUTAMATE RACEMASE FROM AQUIFEX PYROPHILUS===




==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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{{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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