Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor.

Bijàn Mir-Montazeri, Moritz Ammelburg, Dara Forouzan, Andrei N Lupas, Marcus D Hartmann

Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, D-72076 Tübingen, Germany.

Journal of structural biology 2011 Jan

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Proteins of the metallo-β-lactamase (MβL) 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 MβL 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 MβL 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. Copyright © 2010 Elsevier Inc. All rights reserved.

Citation

Bijàn Mir-Montazeri, Moritz Ammelburg, Dara Forouzan, Andrei N Lupas, Marcus D Hartmann. Crystal structure of a dimeric archaeal cleavage and polyadenylation specificity factor. Journal of structural biology. 2011 Jan;173(1):191-5