A novel superfamily containing the beta-grasp fold involved in binding diverse soluble ligands.

ABSTRACT:

Background

Domains containing the beta-grasp fold are utilized in a great diversity of physiological functions but their role, if any, in soluble or small molecule ligand recognition is poorly studied.

Results

Using sensitive sequence and structure similarity searches we identify a novel superfamily containing the beta-grasp fold. They are found in a diverse set of proteins that include the animal vitamin B12 uptake proteins transcobalamin and intrinsic factor, the bacterial polysaccharide export proteins, the competence DNA receptor ComEA, the cob(I)alamin generating enzyme PduS and the Nqo1 subunit of the respiratory electron transport chain. We present evidence that members of this superfamily are likely to bind a range of soluble ligands, including B12. There are two maj

SUBMITTER: Burroughs AM 

PROVIDER: S-EPMC1796856 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature