1qzu
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(New page: 200px<br /> <applet load="1qzu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qzu, resolution 2.91Å" /> '''crystal structure o...)
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Revision as of 16:51, 12 November 2007
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crystal structure of human phosphopantothenoylcysteine decarboxylase
Overview
Phosphopantothenoylcysteine (PPC) decarboxylase is an essential enzyme in, the biosynthesis of coenzyme A and catalyzes the decarboxylation of PPC to, phosphopantetheine. Human PPC decarboxylase has been expressed in, Escherichia coli, purified and crystallized. The Laue class of the, diffraction data appears to be 3m, suggesting space group R32 with two, monomers per asymmetric unit. However, the crystals belong to the space, group R3 and the asymmetric unit contains four monomers. The structure has, been solved using molecular replacement and refined to a current R factor, of 29%. The crystal packing can be considered as two interlaced lattices, each consistent with space group R32 and with the corresponding twofold, axes parallel to each other but separated along the threefold axis. Thus, the true space group is R3 with four monomers per asymmetric unit.
About this Structure
1QZU is a Single protein structure of sequence from Homo sapiens with FMN as ligand. Active as Phosphopantothenoylcysteine decarboxylase, with EC number 4.1.1.36 Full crystallographic information is available from OCA.
Reference
Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase., Manoj N, Ealick SE, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1762-6. Epub 2003, Sep 19. PMID:14501115
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