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'''RNASE P PROTEIN FROM BACILLUS SUBTILIS''' | '''RNASE P PROTEIN FROM BACILLUS SUBTILIS''' | ||
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[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
[[Category: Stams, T.]] | [[Category: Stams, T.]] | ||
[[Category: | [[Category: Endonuclease]] | ||
[[Category: | [[Category: Rnase]] | ||
[[Category: | [[Category: Subunit]] | ||
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Revision as of 06:53, 2 May 2008
RNASE P PROTEIN FROM BACILLUS SUBTILIS
Overview
The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms resolution. This protein binds to ribonuclease P RNA to form a ribonucleoprotein holoenzyme with optimal catalytic activity. Mutagenesis and biochemical data indicate that an unusual left-handed betaalphabeta crossover connection and a large central cleft in the protein form conserved RNA binding sites; a metal binding loop may comprise a third RNA binding site. The unusual topology is partly shared with ribosomal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a common RNA binding ancestor in the primordial translational apparatus.
About this Structure
1A6F is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Ribonuclease P protein structure: evolutionary origins in the translational apparatus., Stams T, Niranjanakumari S, Fierke CA, Christianson DW, Science. 1998 May 1;280(5364):752-5. PMID:9563955 Page seeded by OCA on Fri May 2 09:53:00 2008
