3S4X

Crystal structure of the Asn152Gly mutant of P99 beta-lactamase

3S4X の概要

• エントリーDOI: 10.2210/pdb3s4x/pdb
• 分子名称: Beta-lactamase, SULFATE ION (3 entities in total)
• 機能のキーワード: hydrolase, cephalosporinase
• 由来する生物種: Enterobacter cloacae
• 細胞内の位置: Periplasm (By similarity): P05364
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40754.08

構造登録者

Ruble, J.F.,Powers, R.A. (登録日: 2011-05-20, 公開日: 2012-08-01, 最終更新日: 2023-09-13)

主引用文献

Ruble, J.F.,Lefurgy, S.T.,Cornish, V.W.,Powers, R.A.
Structural analysis of the Asn152Gly mutant of P99 cephalosporinase.
Acta Crystallogr.,Sect.D, 68:1189-1193, 2012

PubMed Abstract: P99 cephalosporinase is a class C β-lactamase that is responsible in part for the widespread bacterial resistance to β-lactam antibiotics. Mutations of the conserved active-site residue Asn152 of the enzyme have been shown to alter β-lactam substrate specificity in vivo. Mutation of Asn152 to a glycine is notable in that it exhibits in vivo substrate-selectivity switching. In order to better understand the structural basis for this observed switch, the X-ray crystal structure of the apo Asn152Gly mutant of P99 was determined to 1.95 Å resolution. Unexpectedly, the artificial C-terminal His(6) tag of a symmetrically-related molecule was observed bound in the active site. The His(6) tag makes several interactions with key active-site residues, as well as with several sulfate ions. Additionally, the overall C-terminus occupies the space left vacant upon the mutation of Asn152 to glycine.

PubMed: 22948919
DOI: 10.1107/S0907444912024080

実験手法

X-RAY DIFFRACTION (1.95 Å)