1p9o
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(New page: 200px<br /> <applet load="1p9o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9o, resolution 2.30Å" /> '''Crystal Structure o...)
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Revision as of 16:35, 12 November 2007
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Crystal Structure of Phosphopantothenoylcysteine Synthetase
Overview
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.
About this Structure
1P9O is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Active as Phosphopantothenate--cysteine ligase, with EC number 6.3.2.5 Full crystallographic information is available from OCA.
Reference
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution., Manoj N, Strauss E, Begley TP, Ealick SE, Structure. 2003 Aug;11(8):927-36. PMID:12906824
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