2XWQ: Anaerobic Cobalt Chelatase From Archeaoglobus Fulgidus ( Cbix) In Complex With Metalated Sirohydrochlorin Product

The class II chelatases associated with heme, siroheme, and cobalamin biosynthesis are structurally related enzymes that insert a specific metal ion (Fe(2+) or Co(2+)) into the center of a modified tetrapyrrole (protoporphyrin or sirohydrochlorin). The structures of two related class II enzymes, CbiX(S) from Archaeoglobus fulgidus and CbiK from Salmonella enterica, that are responsible for the insertion of cobalt along the cobalamin biosynthesis pathway are presented in complex with their metallated product. A further structure of a CbiK from Desulfovibrio vulgaris Hildenborough reveals how cobalt is bound at the active site. The crystal structures show that the binding of sirohydrochlorin is distinctly different to porphyrin binding in the protoporphyrin ferrochelatases and provide a molecular overview of the mechanism of chelation. The structures also give insights into the evolution of chelatase form and function. Finally, the structure of a periplasmic form of Desulfovibrio vulgaris Hildenborough CbiK reveals a novel tetrameric arrangement of its subunits that are stabilized by the presence of a heme b cofactor. Whereas retaining colbaltochelatase activity, this protein has acquired a central cavity with the potential to chaperone or transport metals across the periplasmic space, thereby evolving a new use for an ancient protein subunit.
PDB ID: 2XWQDownload
MMDB ID: 87423
PDB Deposition Date: 2010/11/4
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 2.01  Å
Source Organism:
Similar Structures:
Biological Unit for 2XWQ: dimeric; determined by software (PISA)
Molecular Components in 2XWQ
Label Count Molecule
Proteins (2 molecules)
Sirohydrochlorin Cobaltochelatase(Gene symbol: AF_RS03655)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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