3o3g
From Proteopedia
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- | [[Image:3o3g.png|left|200px]] | ||
- | + | ==T. maritima RNase H2 in complex with nucleic acid substrate and calcium ions== | |
+ | <StructureSection load='3o3g' size='340' side='right'caption='[[3o3g]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3o3g]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O3G FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3g OCA], [https://pdbe.org/3o3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o3g RCSB], [https://www.ebi.ac.uk/pdbsum/3o3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o3g ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RNH2_THEMA RNH2_THEMA] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Two classes of RNase H hydrolyze RNA of RNA/DNA hybrids. In contrast to RNase H1 that requires four ribonucleotides for cleavage, RNase H2 can nick duplex DNAs containing a single ribonucleotide, suggesting different in vivo substrates. We report here the crystal structures of a type 2 RNase H in complex with substrates containing a (5')RNA-DNA(3') junction. They revealed a unique mechanism of recognition and substrate-assisted cleavage. A conserved tyrosine residue distorts the nucleic acid at the junction, allowing the substrate to function in catalysis by participating in coordination of the active site metal ion. The biochemical and structural properties of RNase H2 explain the preference of the enzyme for junction substrates and establish the structural and mechanistic differences with RNase H1. Junction recognition is important for the removal of RNA embedded in DNA and may play an important role in DNA replication and repair. | ||
- | + | Crystal Structures of RNase H2 in Complex with Nucleic Acid Reveal the Mechanism of RNA-DNA Junction Recognition and Cleavage.,Rychlik MP, Chon H, Cerritelli SM, Klimek P, Crouch RJ, Nowotny M Mol Cell. 2010 Nov 24;40(4):658-70. PMID:21095591<ref>PMID:21095591</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3o3g" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[Ribonuclease|Ribonuclease]] | + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
- | [[Category: Cerritelli | + | [[Category: Cerritelli SM]] |
- | [[Category: Chon | + | [[Category: Chon H]] |
- | [[Category: Crouch | + | [[Category: Crouch RJ]] |
- | [[Category: Klimek | + | [[Category: Klimek P]] |
- | [[Category: Nowotny | + | [[Category: Nowotny M]] |
- | [[Category: Rychlik | + | [[Category: Rychlik MP]] |
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Current revision
T. maritima RNase H2 in complex with nucleic acid substrate and calcium ions
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