Structure. 2003 Aug;11(8):927-36.

Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution.

Manoj N, Strauss E, Begley TP, Ealick SE.

Source

Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.

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.

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Structure. 2003 Aug;11(8):899-900.

PMID:: 12906824; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of Phosphopantothenoylcysteine Synthetaseÿ

PDB: 1P9O

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 2.3 Å

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