2hvs: Difference between revisions

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[[Image:2hvs.gif|left|200px]]
{{Seed}}
[[Image:2hvs.png|left|200px]]


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{{STRUCTURE_2hvs|  PDB=2hvs  |  SCENE=  }}  
{{STRUCTURE_2hvs|  PDB=2hvs  |  SCENE=  }}  


'''Structure of T4 RNA Ligase 2 with Nicked 5'-Adenylated nucleic acid duplex containing a 2'-deoxyribonucleotide at the nick'''
===Structure of T4 RNA Ligase 2 with Nicked 5'-Adenylated nucleic acid duplex containing a 2'-deoxyribonucleotide at the nick===




==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}}


==About this Structure==
==About this Structure==
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[[Category: Rna]]
[[Category: Rna]]
[[Category: T4]]
[[Category: T4]]
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