2dkf

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spinqualitylabelsall models 2dkf, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of TTHA0252 from Thermus thermophilus HB8, a RNA Degradation Protein of the Metallo-beta-lactamase Superfamily

Overview

In bacterial RNA metabolism, mRNA degradation is an important process for, gene expression. Recently, a novel ribonuclease (RNase), belonging to the, beta-CASP family within the metallo-beta-lactamase superfamily, was, identified as a functional homologue of RNase E, a major component for, mRNA degradation in Escherichia coli. Here, we have determined the crystal, structure of TTHA0252 from Thermus thermophilus HB8, which represents the, first report of the tertiary structure of a beta-CASP family protein., TTHA0252 comprises two separate domains: a metallo-beta-lactamase domain, and a "clamp" domain. The active site of the enzyme is located in a cleft, between the two domains, which includes two zinc ions coordinated by seven, conserved residues. Although this configuration is similar to those of, other beta-lactamases, TTHA0252 has one conserved His residue, characteristic of the beta-CASP family as a ligand. We also detected, nuclease activity of TTHA0252 against rRNAs of T. thermophilus. Our, results reveal structural and functional aspects of novel RNase E-like, enzymes with a beta-CASP fold.

About this Structure

2DKF is a Single protein structure of sequence from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-beta-lactamase superfamily., Ishikawa H, Nakagawa N, Kuramitsu S, Masui R, J Biochem (Tokyo). 2006 Oct;140(4):535-42. Epub 2006 Aug 31. PMID:16945939

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