Crystallization and preliminary X-ray crystallographic analyses of CMY-1 and CMY-10, plasmidic class C beta-lactamases with extended substrate spectrum.
Plasmid-encoded class C beta-lactamases, including CMY-1 and CMY-10, hydrolyze the lactam bonds of beta-lactam antibiotics, inducing therapeutic failure and a lack of eradication of clinical isolates by third-generation cephalosporins or cephamycins. Therefore, the enzymes are potential targets for developing agents against pathogens isolated from patients suffering from wound infection, urinary tract infection or pneumonia. CMY-1 and CMY-10 were purified and crystallized at 298 K. X-ray diffraction data from CMY-1 and CMY-10 crystals have been collected to 2.5 and 1.5 A resolution, respectively, using synchrotron radiation. The crystals of the two proteins are isomorphous and belong to the primitive monoclinic space group P2(1).
Lee
Sun-Joo
SJ
Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, South Korea.
Kim
Jae Young
JY
Jung
Ha Il
HI
Suh
Pann-Ghill
PG
Lee
Heung-Soo
HS
Lee
Sang Hee
SH
Cha
Sun-Shin
SS
D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods*; D006868:Hydrolysis; D010957:Plasmids / Q000378:metabolism; D013379:Substrate Specificity; D017356:Synchrotrons; D013696:Temperature; D001618:beta-Lactamases / Q000737:chemistry*
C491823:CMY-1 beta-lactamase; C491822:CMY-10 beta-lactamase; D001618:beta-Lactamases