title: Crystallographic studies on B12 binding proteins in eukaryotes and prokaryotes.
abstract: The X-ray crystal structures of several important vitamin B12 binding proteins that have been solved in recent years have enhanced our current understanding in the vitamin B12 field. These structurally diverse groups of B12 binding proteins perform various important biological activities, both by transporting B12 as well as catalyzing various biological reactions. An in-depth comparative analysis of these structures was carried out using PDB coordinates of a carefully chosen database of B12 binding proteins to correlate the overall folding of the molecule with phylogeny, the B12 interactions, and with their biological function. The structures of these proteins are discussed in the context of this comparative analysis.
authors: NE-CAT and Department of Chemistry and Chemical Biology, Cornell University, Building 436E, Argonne National Laboratory, Argonne, IL 60439, USA. sukumar@anl.gov
authors: Narayanasami
authors: N
authors: Sukumar
mesh_terms: D000818:Animals; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D011387:Prokaryotic Cells / Q000378:metabolism*; D011485:Protein Binding; D014155:Transcobalamins / Q000378:metabolism*; D014805:Vitamin B 12 / Q000378:metabolism
chemical_list: D014155:Transcobalamins; D014805:Vitamin B 12
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