2hvq
From Proteopedia
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- | [[Image:2hvq.gif|left|200px]] | + | [[Image:2hvq.gif|left|200px]] |
- | + | ||
- | '''Structure of Adenylated full-length T4 RNA Ligase 2''' | + | {{Structure |
+ | |PDB= 2hvq |SIZE=350|CAPTION= <scene name='initialview01'>2hvq</scene>, resolution 2.400Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= Y10A, 24.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | ||
+ | }} | ||
+ | |||
+ | '''Structure of Adenylated full-length T4 RNA Ligase 2''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2HVQ is a [ | + | 2HVQ 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=2HVQ OCA]. |
==Reference== | ==Reference== | ||
- | RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward., Nandakumar J, Shuman S, Lima CD, Cell. 2006 Oct 6;127(1):71-84. PMID:[http:// | + | RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward., Nandakumar J, Shuman S, Lima CD, Cell. 2006 Oct 6;127(1):71-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17018278 17018278] |
[[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 17:22:14 2008'' |
Revision as of 15:22, 20 March 2008
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, resolution 2.400Å | |||||||
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Ligands: | |||||||
Gene: | Y10A, 24.1 (Bacteriophage T4) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of Adenylated full-length T4 RNA Ligase 2
Overview
T4 RNA ligase 2 (Rnl2) and kinetoplastid RNA editing ligases exemplify a family of RNA repair enzymes that seal 3'OH/5'PO(4) nicks in duplex RNAs via ligase adenylylation (step 1), AMP transfer to the nick 5'PO(4) (step 2), and attack by the nick 3'OH on the 5'-adenylylated strand to form a phosphodiester (step 3). Crystal structures are reported for Rnl2 at discrete steps along this pathway: the covalent Rnl2-AMP intermediate; Rnl2 bound to an adenylylated nicked duplex, captured immediately following step 2; and Rnl2 at an adenylylated nick in a state poised for step 3. These structures illuminate the stereochemistry of nucleotidyl transfer and reveal how remodeling of active-site contacts and conformational changes propel the ligation reaction forward. Mutational analysis and comparison of nick-bound structures of Rnl2 and human DNA ligase I highlight common and divergent themes of substrate recognition that can explain their specialization for RNA versus DNA repair.
About this Structure
2HVQ is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forward., Nandakumar J, Shuman S, Lima CD, Cell. 2006 Oct 6;127(1):71-84. PMID:17018278
Page seeded by OCA on Thu Mar 20 17:22:14 2008
Categories: Bacteriophage t4 | Single protein | Lima, C D. | Nandakumar, J. | MG | Ligase | Lysine adenylate | Rna | T4