1nz0

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spinqualitylabelsall models 1nz0, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RNASE P PROTEIN FROM THERMOTOGA MARITIMA

Overview

The structure of RNase P protein from the hyperthermophilic bacterium, Thermotoga maritima was determined at 1.2-A resolution by using x-ray, crystallography. This protein structure is from an ancestral-type RNase P, and bears remarkable similarity to the recently determined structures of, RNase P proteins from bacteria that have the distinct, Bacillus type of, RNase P. These two types of protein span the extent of bacterial RNase P, diversity, so the results generalize the structure of the bacterial RNase, P protein. The broad phylogenetic conservation of structure and, distribution of potential RNA-binding elements in the RNase P proteins, indicate that all of these homologous proteins bind to their cognate RNAs, primarily by interaction with the phylogenetically conserved core of the, RNA. The protein is found to dimerize through an extensive, well-ordered, interface. This dimerization may reflect a mechanism of thermal stability, of the protein before assembly with the RNA moiety of the holoenzyme.

About this Structure

1NZ0 is a Single protein structure of sequence from Thermotoga maritima with SO4 as ligand. Active as Ribonuclease P, with EC number 3.1.26.5 Full crystallographic information is available from OCA.

Reference

High-resolution structure of RNase P protein from Thermotoga maritima., Kazantsev AV, Krivenko AA, Harrington DJ, Carter RJ, Holbrook SR, Adams PD, Pace NR, Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7497-502. Epub 2003 Jun 10. PMID:12799461

Page seeded by OCA on Tue Nov 20 22:40:23 2007