1P9O

Crystal Structure of Phosphopantothenoylcysteine Synthetase

Summary for 1P9O

• Entry DOI: 10.2210/pdb1p9o/pdb
• Descriptor: Phosphopantothenoylcysteine synthetase, SULFATE ION (3 entities in total)
• Functional Keywords: synthetase, ligase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 68520.48

Authors

Manoj, N.,Strauss, E.,Begley, T.P.,Ealick, S.E. (deposition date: 2003-05-12, release date: 2003-09-02, Last modification date: 2024-04-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)