1P9O

Crystal Structure of Phosphopantothenoylcysteine Synthetase

1P9O の概要

• エントリーDOI: 10.2210/pdb1p9o/pdb
• 分子名称: Phosphopantothenoylcysteine synthetase, SULFATE ION (3 entities in total)
• 機能のキーワード: synthetase, ligase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68520.48

構造登録者

Manoj, N.,Strauss, E.,Begley, T.P.,Ealick, S.E. (登録日: 2003-05-12, 公開日: 2003-09-02, 最終更新日: 2024-04-03)

主引用文献

Manoj, N.,Strauss, E.,Begley, T.P.,Ealick, S.E.
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution.
Structure, 11:927-936, 2003

PubMed Abstract: The structure of human phosphopantothenoylcysteine (PPC) synthetase was determined at 2.3 A 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 ATP binding residues include Gly43, Ser61, Gly63, Gly66, Phe230, and Asn258. Highly conserved phosphopantothenate binding residues include Asn59, Ala179, Ala180, 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.

PubMed: 12906824
DOI: 10.1016/S0969-2126(03)00146-1

実験手法

X-RAY DIFFRACTION (2.3 Å)