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| {{STRUCTURE_2hvq| PDB=2hvq | SCENE= }} | | {{STRUCTURE_2hvq| PDB=2hvq | SCENE= }} |
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| '''Structure of Adenylated full-length T4 RNA Ligase 2'''
| | ===Structure of Adenylated full-length T4 RNA Ligase 2=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17018278}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17018278 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17018278}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rna]] | | [[Category: Rna]] |
| [[Category: T4]] | | [[Category: T4]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:46:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:17:02 2008'' |
