1oqk: Difference between revisions

Revision as of 19:00, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oqk.png

Template:STRUCTURE 1oqk

Structure of Mth11: A homologue of human RNase P protein Rpp29Structure of Mth11: A homologue of human RNase P protein Rpp29

Template:ABSTRACT PUBMED 14673079

About this StructureAbout this Structure

1OQK is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full experimental information is available from OCA.

ReferenceReference

Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P., Boomershine WP, McElroy CA, Tsai HY, Wilson RC, Gopalan V, Foster MP, Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15398-403. Epub 2003 Dec 12. PMID:14673079

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-'''Structure of Mth11: A homologue of human RNase P protein Rpp29'''
+===Structure of Mth11: A homologue of human RNase P protein Rpp29===
-==Overview==
+<!--
-We have determined the solution structure of Mth11 (Mth Rpp29), an essential subunit of the RNase P enzyme from the archaebacterium Methanothermobacter thermoautotrophicus (Mth). RNase P is a ubiquitous ribonucleoprotein enzyme primarily responsible for cleaving the 5' leader sequence during maturation of tRNAs in all three domains of life. In eubacteria, this enzyme is made up of two subunits: a large RNA ( approximately 120 kDa) responsible for mediating catalysis, and a small protein cofactor ( approximately 15 kDa) that modulates substrate recognition and is required for efficient in vivo catalysis. In contrast, multiple proteins are associated with eukaryotic and archaeal RNase P, and these proteins exhibit no recognizable homology to the conserved bacterial protein subunit. In reconstitution experiments with recombinantly expressed and purified protein subunits, we found that Mth Rpp29, a homolog of the Rpp29 protein subunit from eukaryotic RNase P, is an essential protein component of the archaeal holoenzyme. Consistent with its role in mediating protein-RNA interactions, we report that Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. In addition to a structured beta-barrel core, it possesses unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues. To identify possible RNA contacts in the protein-RNA complex, we examined the interaction of the 11-kDa protein with the full 100-kDa Mth RNA subunit by using NMR chemical shift perturbation. Our findings represent a critical step toward a structural model of the RNase P holoenzyme from archaebacteria and higher organisms.
+The line below this paragraph, {{ABSTRACT_PUBMED_14673079}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14673079 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14673079}}
 ==About this Structure==
-OQK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQK OCA].
+OQK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQK OCA].
 ==Reference==
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 [[Category: Archaeal rnase p protein subunit]]
 [[Category: Ob fold]]
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