3bk2
From Proteopedia
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caption="3bk2, resolution 2.100Å" /> | caption="3bk2, resolution 2.100Å" /> | ||
'''Crystal Structure Analysis of the RNase J/UMP complex'''<br /> | '''Crystal Structure Analysis of the RNase J/UMP complex'''<br /> | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
| - | 3BK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=U5P:'>U5P</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK2 OCA]. | + | 3BK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=U5P:'>U5P</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+947'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+948'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+A+949'>AC3</scene>, <scene name='pdbsite=AC4:U5p+Binding+Site+For+Residue+A+950'>AC4</scene>, <scene name='pdbsite=AC5:Gol+Binding+Site+For+Residue+A+601'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+A+602'>AC6</scene> and <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+A+603'>AC7</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK2 OCA]. |
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| + | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18204464 18204464] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Putzer, H.]] | [[Category: Putzer, H.]] | ||
| - | [[Category: Sierra-Gallay, I | + | [[Category: Sierra-Gallay, I L.de la.]] |
[[Category: Zig, L.]] | [[Category: Zig, L.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: rnase j]] | [[Category: rnase j]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 27 07:48:46 2008'' |
Revision as of 05:48, 27 February 2008
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Crystal Structure Analysis of the RNase J/UMP complex
Overview
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.
About this Structure
3BK2 is a Single protein structure of sequence from Thermus thermophilus with , , and as ligands. Known structural/functional Sites: , , , , , and . 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
Page seeded by OCA on Wed Feb 27 07:48:46 2008
