青霉素V酰基转移酶自蛋白水解加工突变体的克隆、制备及初步晶体学研究
Cloning, preparation and preliminary crystallographic studies of penicillin V acylase autoproteolytic processing mutants.
作者信息
Chandra P Manish, Brannigan James A, Prabhune Asmita, Pundle Archana, Turkenburg Johan P, Dodson G Guy, Suresh C G
机构信息
Division of Biochemical Sciences, National Chemical Laboratory, Pune 411008, India.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):124-7. doi: 10.1107/S1744309104031227. Epub 2004 Dec 24.
Abstract
The crystallization of three catalytically inactive mutants of penicillin V acylase (PVA) from Bacillus sphaericus in precursor and processed forms is reported. The mutant proteins crystallize in different primitive monoclinic space groups that are distinct from the crystal forms for the native enzyme. Directed mutants and clone constructs were designed to study the post-translational autoproteolytic processing of PVA. The catalytically inactive mutants will provide three-dimensional structures of precursor PVA forms, plus open a route to the study of enzyme-substrate complexes for this industrially important enzyme.
摘要
报道了来自球形芽孢杆菌的青霉素V酰基转移酶（PVA）三种催化失活突变体以前体形式和加工形式的结晶情况。突变蛋白在不同的原始单斜晶系空间群中结晶，这些空间群与天然酶的晶体形式不同。设计了定向突变体和克隆构建体来研究PVA的翻译后自蛋白水解加工。催化失活突变体将提供前体PVA形式的三维结构，并为研究这种具有重要工业价值的酶的酶-底物复合物开辟一条途径。
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