2e7y | pdb_00002e7y

High resolution structure of T. maritima tRNase Z

File:2e7y.jpg

spinqualitylabelsall models 2e7y, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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 ZN, SO4 and PGO 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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