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3bk1

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{{STRUCTURE_3bk1| PDB=3bk1 | SCENE= }}
{{STRUCTURE_3bk1| PDB=3bk1 | SCENE= }}
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'''Crystal Structure Analysis of RNase J'''
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===Crystal Structure Analysis of RNase J===
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==Overview==
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The maturation and stability of RNA transcripts is controlled by a combination of endo- and exoRNases. RNase J is unique, as it combines an RNase E-like endoribonucleolytic and a 5'-to-3' exoribonucleolytic activity in a single polypeptide. The structural basis for this dual activity is unknown. Here we report the crystal structures of Thermus thermophilus RNase J and its complex with uridine 5'-monophosphate. A binding pocket coordinating the phosphate and base moieties of the nucleotide in the vicinity of the catalytic center provide a rationale for the 5'-monophosphate-dependent 5'-to-3' exoribonucleolytic activity. We show that this dependence is strict; an initial 5'-PPP transcript cannot be degraded exonucleolytically from the 5'-end. Our results suggest that RNase J might switch promptly from endo- to exonucleolytic mode on the same RNA, a property that has important implications for RNA metabolism in numerous prokaryotic organisms and plant organelles containing RNase J orthologs.
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(as it appears on PubMed at http://www.pubmed.gov), where 18204464 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18204464}}
==About this Structure==
==About this Structure==
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[[Category: Metallo-beta-lactamase]]
[[Category: Metallo-beta-lactamase]]
[[Category: Rnase j]]
[[Category: Rnase j]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:52:09 2008''
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Revision as of 00:56, 28 July 2008

Image:3bk1.png

Template:STRUCTURE 3bk1

Crystal Structure Analysis of RNase J

Template:ABSTRACT PUBMED 18204464

About this Structure

3BK1 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural insights into the dual activity of RNase J., de la Sierra-Gallay IL, Zig L, Jamalli A, Putzer H, Nat Struct Mol Biol. 2008 Feb;15(2):206-12. Epub 2008 Jan 20. PMID:18204464

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