2E7Y

High resolution structure of T. maritima tRNase Z

Summary for 2E7Y

• Entry DOI: 10.2210/pdb2e7y/pdb
• Descriptor: tRNase Z, ZINC ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: rnase, trna maturation, metallo-beta-lactamse, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 66185.35

Authors

Ishii, R.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-01-15, release date: 2007-09-11, Last modification date: 2023-10-25)

Primary citation

Ishii, R.,Minagawa, A.,Takaku, H.,Takagi, M.,Nashimoto, M.,Yokoyama, S.
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes
Acta Crystallogr.,Sect.F, 63:637-641, 2007

PubMed Abstract: 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.

PubMed: 17671357
DOI: 10.1107/S1744309107033623

Experimental method

X-RAY DIFFRACTION (1.97 Å)