2p74
From Proteopedia
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CTX-M-9 class A beta-lactamase apo crystal structure at 0.88 Angstrom resolution
Overview
The apo crystal structure of CTX-M-9 beta-lactamase has been determined to, 0.88 A at pH 8.8. This unusually clear picture of proton positions and, residue interactions supports the role of Glu166 as the general base for, the controversial acylation step of class A beta-lactamase catalysis. The, ability to distinguish low-energy conformations sampled by the enzyme, allows us to link the two conformations of Lys73 to different protonation, states of Glu166.
About this Structure
2P74 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
The Acylation Mechanism of CTX-M beta-Lactamase at 0.88 A Resolution., Chen Y, Bonnet R, Shoichet BK, J Am Chem Soc. 2007 Apr 5;. PMID:17408273
Page seeded by OCA on Wed Jan 23 15:19:55 2008
Categories: Beta-lactamase | Escherichia coli | Single protein | Bonnet, R. | Chen, Y. | Shoichet, B.K. | K | PO4 | Acylation | Ctx-m | Esbl | Ultra-high resolution
