2XR1

DIMERIC ARCHAEAL CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR WITH N-TERMINAL KH DOMAINS (KH-CPSF) FROM METHANOSARCINA MAZEI

Summary for 2XR1

• Entry DOI: 10.2210/pdb2xr1/pdb
• Descriptor: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 100 KD SUBUNIT, ZINC ION (3 entities in total)
• Functional Keywords: hydrolase, metallo-beta-lactamase, beta-casp, rna processing
• Biological source: METHANOSARCINA MAZEI
• Total number of polymer chains: 2
• Total formula weight: 144523.82

Authors

Mir-Montazeri, B.,Ammelburg, M.,Forouzan, D.,Lupas, A.N.,Hartmann, M.D. (deposition date: 2010-09-08, release date: 2010-10-06, Last modification date: 2023-12-20)

Primary citation

Mir-Montazeri, B.,Ammelburg, M.,Forouzan, D.,Lupas, A.N.,Hartmann, M.D.
Crystal Structure of a Dimeric Archaeal Cleavage and Polyadenylation Specificity Factor.
J.Struct.Biol., 173:191-, 2011

PubMed Abstract: 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.

PubMed: 20851187
DOI: 10.1016/J.JSB.2010.09.013

Experimental method

X-RAY DIFFRACTION (2.59 Å)