1qgo
From Proteopedia
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ANAEROBIC COBALT CHELATASE IN COBALAMIN BIOSYNTHESIS FROM SALMONELLA TYPHIMURIUM
Overview
Prosthetic groups such as heme, chlorophyll, and cobalamin (vitamin B(12)), are characterized by their branched biosynthetic pathway and unique metal, insertion steps. The metal ion chelatases can be broadly classed either as, single-subunit ATP-independent enzymes, such as the anaerobic cobalt, chelatase and the protoporphyrin IX (PPIX) ferrochelatase, or as, heterotrimeric, ATP-dependent enzymes, such as the Mg chelatase involved, in chlorophyll biosynthesis. The X-ray structure of the anaerobic cobalt, chelatase from Salmonella typhimurium, CbiK, has been solved to 2.4 A, resolution. Despite a lack of significant amino acid sequence similarity, the protein structure is homologous to that of Bacillus subtilis PPIX, ferrochelatase. Both enzymes contain a histidine residue previously, ... [(full description)]
About this Structure
1QGO is a [Single protein] structure of sequence from [Salmonella typhimurium] with SO4 as [ligand]. Structure known Active Site: CO. Full crystallographic information is available from [OCA].
Reference
Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis., Schubert HL, Raux E, Wilson KS, Warren MJ, Biochemistry. 1999 Aug 17;38(33):10660-9. PMID:10451360
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