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• W2023341649 endingPage "301" @default.
• W2023341649 startingPage "289" @default.
• W2023341649 abstract "Bacterial β-lactamases hydrolyze β-lactam antibiotics such as penicillins and cephalosporins. The TEM-type class A β-lactamase SHV-2 is a natural variant that exhibits activity against third-generation cephalosporins normally resistant to hydrolysis by class A enzymes. SHV-2 contains a single Gly238Ser change relative to the wild-type enzyme SHV-1. Crystallographic refinement of a model including hydrogen atoms gave R and Rfree of 12.4% and 15.0% for data to 0.91 Å resolution. The hydrogen atom on the Oγ atom of the reactive Ser70 is clearly seen for the first time, bridging to the water molecule activated by Glu166. Though hydrogen atoms on the nearby Lys73 are not seen, this observation of the Ser70 hydrogen atom and the hydrogen bonding pattern around Lys73 indicate that Lys73 is protonated. These findings support a role for the Glu166–water couple, rather than Lys73, as the general base in the deprotonation of Ser70 in the acylation process of class A β-lactamases. Overlay of SHV-2 with SHV-1 shows a significant 1–3 Å displacement in the 238–242 β-strand-turn segment, making the β-lactam binding site more open to newer cephalosporins with large C7 substituents and thereby expanding the substrate spectrum of the variant enzyme. The OH group of the buried Ser238 side-chain hydrogen bonds to the main-chain CO of Asn170 on the Ω loop, that is unaltered in position relative to SHV-1. This structural role for Ser238 in protein–protein binding makes less likely its hydrogen bonding to oximino cephalosporins such as cefotaxime or ceftazidime." @default.
• W2023341649 created "2016-06-24" @default.
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• W2023341649 date "2003-04-01" @default.
• W2023341649 modified "2023-09-26" @default.
• W2023341649 title "Ultrahigh Resolution Structure of a Class A β-Lactamase: On the Mechanism and Specificity of the Extended-spectrum SHV-2 Enzyme" @default.
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• W2023341649 doi "https://doi.org/10.1016/s0022-2836(03)00210-9" @default.
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