3bfg
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(New page: 200px<br /><applet load="3bfg" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bfg, resolution 2.0Å" /> '''class A beta-lactamas...)
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Revision as of 09:37, 23 January 2008
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class A beta-lactamase SED-G238C complexed with meropenem
Overview
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type, extended-spectrum beta-lactamase that has the ability to hydrolyze, expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED, mutant in which Gly238 has been replaced by a cysteine, forming a, disulfide bridge with the other Cys residue located at position 69, (SED-G238C), have been crystallized. The crystals belong to the monoclinic, space group C2, with unit-cell parameters a = 188.09, b = 73.65, c =, 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c =, 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray, diffraction data were collected to maximum resolutions of 2.4 A for SED-1, and 2.0 A for SED-G238C.
About this Structure
3BFG is a Single protein structure of sequence from Citrobacter sedlakii with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii., Petrella S, Pernot L, Sougakoff W, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):125-8. Epub 2003, Dec 18. PMID:14684905
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