2AFV

The Crystal Structure of Putative Precorrin Isomerase CbiC in Cobalamin Biosynthesis

Summary for 2AFV

• Entry DOI: 10.2210/pdb2afv/pdb
• Related: 2AFR
• Descriptor: cobalamin biosynthesis precorrin isomerase, CHLORIDE ION, HEXAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: isomerase
• Biological source: Leptospira interrogans
• Total number of polymer chains: 2
• Total formula weight: 52668.10

Authors

Xue, Y.,Wei, Z. (deposition date: 2005-07-26, release date: 2006-04-04, Last modification date: 2024-03-13)

Primary citation

Xue, Y.,Wei, Z.,Li, X.,Gong, W.
The crystal structure of putative precorrin isomerase CbiC in cobalamin biosynthesis
J.Struct.Biol., 153:307-311, 2006

PubMed Abstract: The leptospira cbiC encodes the enzyme catalyzing the methyl rearrangement reaction of the cobalamin biosynthesis pathway. The protein has been cloned and overexpressed as a His-tagged recombinant protein in Escherichia coli. The crystal structures have been solved in two crystal forms (P4(2)2(1)2 and P3(1)21) diffracting to 3.0 and 2.3A resolution, respectively. The structures are similar to the precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12.

PubMed: 16427313
DOI: 10.1016/j.jsb.2005.11.011

Experimental method

X-RAY DIFFRACTION (3 Å)