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5a0v
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Catalysis and 5' end sensing by ribonuclease RNase J of the metallo- beta-lactamase family== |
| + | <StructureSection load='5a0v' size='340' side='right' caption='[[5a0v]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5a0v]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A0V FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a0t|5a0t]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a0v RCSB], [http://www.ebi.ac.uk/pdbsum/5a0v PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In diverse bacterial species, the turnover and processing of many RNAs is mediated by the ribonuclease RNase J, a member of the widely occurring metallo-beta-lactamase enzyme family. We present crystal structures of Streptomyces coelicolor RNase J with bound RNA in pre- and post-cleavage states, at 2.27 A and 2.80 A resolution, respectively. These structures reveal snapshots of the enzyme cleaving substrate directionally and sequentially from the 5' terminus. In the pre-cleavage state, a water molecule is coordinated to a zinc ion pair in the active site but is imperfectly oriented to launch a nucleophilic attack on the phosphate backbone. A conformational switch is envisaged that enables the in-line positioning of the attacking water and may be facilitated by magnesium ions. Adjacent to the scissile bond, four bases are stacked in a tightly sandwiching pocket, and mutagenesis results indicate that this organization helps to drive processive exo-ribonucleolytic cleavage. Like its numerous homologues, S. coelicolor RNase J can also cleave some RNA internally, and the structural data suggest how the preference for exo- versus endo-cleavage mode is linked with recognition of the chemical status of the substrate's 5' end. | ||
| - | + | Linkage of catalysis and 5' end recognition in ribonuclease RNase J.,Pei XY, Bralley P, Jones GH, Luisi BF Nucleic Acids Res. 2015 Aug 7. pii: gkv732. PMID:26253740<ref>PMID:26253740</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
[[Category: Bralley, P]] | [[Category: Bralley, P]] | ||
| - | [[Category: Jones, G | + | [[Category: Jones, G H]] |
| + | [[Category: Luisi, B F]] | ||
| + | [[Category: Pei, X Y]] | ||
| + | [[Category: Endonuclease]] | ||
| + | [[Category: Exonuclease]] | ||
| + | [[Category: Hydrolase-rna complex]] | ||
Revision as of 12:19, 20 August 2015
Catalysis and 5' end sensing by ribonuclease RNase J of the metallo- beta-lactamase family
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