1qzu

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crystal structure of human phosphopantothenoylcysteine decarboxylase

Structural highlights

1qzu is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.91Å
Ligands:FMN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COAC_HUMAN Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'-phosphopantotheine.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. ↑ Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A. Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. PMID:11923312 doi:http://dx.doi.org/10.1074/jbc.M201708200
  2. ↑ Strauss E, Zhai H, Brand LA, McLafferty FW, Begley TP. Mechanistic studies on phosphopantothenoylcysteine decarboxylase: trapping of an enethiolate intermediate with a mechanism-based inactivating agent. Biochemistry. 2004 Dec 14;43(49):15520-33. PMID:15581364 doi:http://dx.doi.org/10.1021/bi048340a
  3. ↑ Manoj N, Ealick SE. Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1762-6. Epub 2003, Sep 19. PMID:14501115

Contents


PDB ID 1qzu

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