3bk2
From Proteopedia
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|PDB= 3bk2 |SIZE=350|CAPTION= <scene name='initialview01'>3bk2</scene>, resolution 2.100Å | |PDB= 3bk2 |SIZE=350|CAPTION= <scene name='initialview01'>3bk2</scene>, resolution 2.100Å | ||
|SITE= <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> | |SITE= <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> | ||
- | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=U5P:URIDINE-5 | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=U5P:URIDINE-5'-MONOPHOSPHATE'>U5P</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TTC0775 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |GENE= TTC0775 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
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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 Sun Mar 23 16:00:00 2008'' |
Revision as of 14:00, 23 March 2008
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, resolution 2.100Å | |||||||
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Sites: | , , , , , and | ||||||
Ligands: | , , and | ||||||
Gene: | TTC0775 (Thermus thermophilus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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