2xr1

Publication Abstract from PubMed

Proteins of the metallo-beta-lactamase (MbetaL) fold form a large superfamily of metallo-hydrolase/oxidoreductases. Members of this family are found in all three domains of life and are involved in a variety of biological functions related to hydrolysis, redox processes, DNA repair and uptake, and RNA processing. We classified the archaeal homologs of this superfamily based on sequence similarity and characterized a subfamily of the Cleavage and Polyadenylation Specificity Factor (CPSF) with an uncommon domain composition: in addition to an extended MbetaL domain, which accommodates the active site for RNA cleavage, this group has two N-terminal KH domains. Here, we present the crystal structure of a member of this group from Methanosarcina mazei. It reveals a dimerization mode of the MbetaL domain that has not been observed before and suggests that RNA is bound across the dimer interface, recognized by the KH domains of one monomer, and cleaved at the active site of the other.

Crystal structure of a dimeric archaeal Cleavage and Polyadenylation Specificity Factor.,Mir-Montazeri B, Ammelburg M, Forouzan D, Lupas AN, Hartmann MD J Struct Biol. 2010 Sep 17. PMID:20851187^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.