2e7y

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Revision as of 11:38, 23 January 2008

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spinqualitylabelsall models 2e7y, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

High resolution structure of T. maritima tRNase Z

Overview

tRNA 3'-processing endoribonuclease (tRNase Z) is one of the enzymes, involved in the 3'-end processing of precursor tRNAs and is a member of, the metallo-beta-lactamase superfamily. tRNase Z crystal structures have, revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the, metallo-beta-lactamase core and is involved in tRNA binding. The refined, structure of Thermotoga maritima tRNase Z has been determined at 1.97 A, resolution, revealing the structure of the flexible arm and the zinc-bound, active site. The structure of the flexible arm of T. maritima tRNase Z is, distinct from those of the Bacillus subtilis and Escherichia coli tRNase, Zs. A comparison of the three tRNase Z structures revealed differences in, the dimer orientation, which may be related to the unique cleavage-site, specificity of T. maritima tRNase Z.

About this Structure

2E7Y is a Single protein structure of sequence from Thermotoga maritima with , and as ligands. Active as Ribonuclease Z, with EC number 3.1.26.11 Full crystallographic information is available from OCA.

Reference

The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes., Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):637-41. Epub 2007 Jul 21. PMID:17671357

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