Publication Date:
2010-11-16
Description:
Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA(Phe). The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA-RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5' leader sequence with and without metal help to identify the 5' substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of catalysis by RNase P.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058908/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058908/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reiter, Nicholas J -- Osterman, Amy -- Torres-Larios, Alfredo -- Swinger, Kerren K -- Pan, Tao -- Mondragon, Alfonso -- F32 GM087055/GM/NIGMS NIH HHS/ -- R01 GM058443/GM/NIGMS NIH HHS/ -- R01 GM058443-12/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Dec 9;468(7325):784-9. doi: 10.1038/nature09516. Epub 2010 Nov 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21076397" target="_blank"〉PubMed〈/a〉
Keywords:
Biocatalysis
;
Catalytic Domain
;
Crystallography, X-Ray
;
Genes, Bacterial/genetics
;
Holoenzymes/chemistry/genetics/metabolism
;
Metals/metabolism
;
Models, Molecular
;
Molecular Conformation
;
RNA, Transfer, Phe/chemistry/genetics/*metabolism
;
Ribonuclease P/*chemistry/genetics/*metabolism
;
Structure-Activity Relationship
;
Substrate Specificity
;
Thermotoga maritima/*enzymology/genetics
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
