Structure of human phosphopantothenoylcysteine synthetase at 2.3 Å resolution

被引：27

作者：

Manoj, N ^{[1
]}

Strauss, E ^{[1
]}

Begley, TP ^{[1
]}

Ealick, SE ^{[1
]}

机构：

[1] Cornell Univ, Dept Chem & Chem Biol, Ithaca, NY 14853 USA

来源：

STRUCTURE | 2003年 / 11卷 / 08期

关键词：

D O I：

10.1016/S0969-2126(03)00146-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 Angstrom resolution. PPC synthetase is a dimer with identical monomers. Some features of the monomer fold resemble a group of NAD-dependent enzymes, while other features resemble the ribokinase fold. The ATP, phosphopantothenate, and cysteine binding sites were deduced from modeling studies. Highly conserved ATIP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, AIa180, and Asp183 from one monomer and Arg55' from the adjacent monomer. The structure predicts a ping pong mechanism with initial formation of an acyladenylate intermediate followed by release of pyrophosphate and attack by; cysteine to form the final products PPC and AMP.

引用

页码：927 / 936

页数：10

共 38 条

[1] Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self-processing [J].