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3bk1
From Proteopedia
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| - | [[Image:3bk1.jpg|left|200px]] | + | [[Image:3bk1.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal Structure Analysis of RNase J''' | + | {{Structure |
| + | |PDB= 3bk1 |SIZE=350|CAPTION= <scene name='initialview01'>3bk1</scene>, resolution 2.330Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+945'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+946'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+947'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+A+948'>AC4</scene>, <scene name='pdbsite=AC5:Zn+Binding+Site+For+Residue+A+949'>AC5</scene>, <scene name='pdbsite=AC6:Gol+Binding+Site+For+Residue+A+601'>AC6</scene> and <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+A+602'>AC7</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= TTC0775 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Analysis of RNase J''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BK1 is a [ | + | 3BK1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BK1 OCA]. |
==Reference== | ==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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/18204464 18204464] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: 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 Thu Mar 20 18:59:38 2008'' |
Revision as of 16:59, 20 March 2008
| |||||||
| , resolution 2.330Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , and | ||||||
| Gene: | TTC0775 (Thermus thermophilus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of RNase J
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
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
Page seeded by OCA on Thu Mar 20 18:59:38 2008
