1s68: Difference between revisions
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[[Image:1s68.jpg|left|200px]] | [[Image:1s68.jpg|left|200px]] | ||
'''Structure and Mechanism of RNA Ligase''' | {{Structure | ||
|PDB= 1s68 |SIZE=350|CAPTION= <scene name='initialview01'>1s68</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | |||
|ACTIVITY= | |||
|GENE= Y10A, 24.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | |||
}} | |||
'''Structure and Mechanism of RNA Ligase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1S68 is a [ | 1S68 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S68 OCA]. | ||
==Reference== | ==Reference== | ||
Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:[http:// | Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14962393 14962393] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: t4]] | [[Category: t4]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:02 2008'' |
Revision as of 15:01, 20 March 2008
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, resolution 1.90Å | |||||||
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Ligands: | |||||||
Gene: | Y10A, 24.1 (Bacteriophage T4) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure and Mechanism of RNA Ligase
OverviewOverview
T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.
About this StructureAbout this Structure
1S68 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:14962393
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