1lrz
From Proteopedia
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(New page: 200px<br /><applet load="1lrz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lrz, resolution 2.10Å" /> '''x-ray crystal struct...)
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Revision as of 18:42, 20 November 2007
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x-ray crystal structure of staphylococcus aureus femA
Overview
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.
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
Page seeded by OCA on Tue Nov 20 20:49:32 2007
