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| ==T. maritima RNase H2 D107N in complex with nucleic acid substrate and manganese ions== | | ==T. maritima RNase H2 D107N in complex with nucleic acid substrate and manganese ions== |
| <StructureSection load='3o3h' size='340' side='right' caption='[[3o3h]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3o3h' size='340' side='right'caption='[[3o3h]], [[Resolution|resolution]] 2.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3o3h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O3H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O3H FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3o3h]] 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=3O3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O3H FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2etj|2etj]], [[3o3f|3o3f]], [[3o3g|3o3g]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnhB, TM_0915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=3o3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3h OCA], [https://pdbe.org/3o3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o3h RCSB], [https://www.ebi.ac.uk/pdbsum/3o3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o3h ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span></td></tr>
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| <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=3o3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o3h RCSB], [http://www.ebi.ac.uk/pdbsum/3o3h PDBsum]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RNH2_THEMA RNH2_THEMA]] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity). | | [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;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Ribonuclease|Ribonuclease]] | | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] |
| *[[Temp|Temp]]
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| *[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Ribonuclease H]] | | [[Category: Large Structures]] |
| [[Category: Thermotoga maritima]] | | [[Category: Thermotoga maritima]] |
| [[Category: Cerritelli, S M]] | | [[Category: Cerritelli SM]] |
| [[Category: Chon, H]] | | [[Category: Chon H]] |
| [[Category: Crouch, R J]] | | [[Category: Crouch RJ]] |
| [[Category: Klimek, P]] | | [[Category: Klimek P]] |
| [[Category: Nowotny, M]] | | [[Category: Nowotny M]] |
| [[Category: Rychlik, M P]] | | [[Category: Rychlik MP]] |
| [[Category: Hydrolase-dna-rna hybrid complex]]
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| [[Category: Nuclease]]
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| [[Category: Rnase h fold]]
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