1lrz

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{{STRUCTURE_1lrz| PDB=1lrz | SCENE= }}
{{STRUCTURE_1lrz| PDB=1lrz | SCENE= }}
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'''x-ray crystal structure of staphylococcus aureus femA'''
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===x-ray crystal structure of staphylococcus aureus femA===
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==Overview==
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The latter stages of peptidoglycan biosynthesis in Staphylococci involve the synthesis of a pentaglycine bridge on the epsilon amino group of the pentapeptide lysine side chain. Genetic and biochemical evidence suggest that sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA, and FemB. The first protein structure from this family, Staphylococcus aureus FemA, has been solved at 2.1 A resolution by X-ray crystallography. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein also reveals an L-shaped channel suitable for a peptidoglycan substrate. Analysis of the structural features of this enzyme provides clues to the mechanism of action of S. aureus FemA.
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(as it appears on PubMed at http://www.pubmed.gov), where 12176388 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12176388}}
==About this Structure==
==About this Structure==
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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Revision as of 18:56, 2 July 2008

Image:1lrz.png

Template:STRUCTURE 1lrz

x-ray crystal structure of staphylococcus aureus femA

Template:ABSTRACT PUBMED 12176388

About this Structure

1LRZ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of Staphylococcus aureus FemA., Benson TE, Prince DB, Mutchler VT, Curry KA, Ho AM, Sarver RW, Hagadorn JC, Choi GH, Garlick RL, Structure. 2002 Aug;10(8):1107-15. PMID:12176388

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