title: The crystal structure of putative precorrin isomerase CbiC in cobalamin biosynthesis.
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.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, PR China.
authors.forename: Yanyan
authors.initials: Y
authors.lastname: Xue
authors.forename: Zhiyi
authors.initials: Z
authors.lastname: Wei
authors.forename: Xu
authors.initials: X
authors.lastname: Li
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D007535:Isomerases / Q000737:chemistry*; D007921:Leptospira interrogans / Q000201:enzymology*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D014805:Vitamin B 12 / Q000096:biosynthesis*
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D007535:Isomerases; D014805:Vitamin B 12