3o3h

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<StructureSection load='3o3h' size='340' side='right'caption='[[3o3h]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3o3h' size='340' side='right'caption='[[3o3h]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o3h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. 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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2etj|2etj]], [[3o3f|3o3f]], [[3o3g|3o3g]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnhB, TM_0915 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [https://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'>[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='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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RNH2_THEMA RNH2_THEMA]] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity).
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[https://www.uniprot.org/uniprot/RNH2_THEMA RNH2_THEMA] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity).
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<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3o3h" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ribonuclease H]]
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[[Category: Thermotoga maritima]]
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[[Category: Cerritelli, S M]]
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[[Category: Cerritelli SM]]
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[[Category: Chon, H]]
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[[Category: Chon H]]
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[[Category: Crouch, R J]]
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[[Category: Crouch RJ]]
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[[Category: Klimek, P]]
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[[Category: Klimek P]]
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[[Category: Nowotny, M]]
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[[Category: Nowotny M]]
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[[Category: Rychlik, M P]]
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[[Category: Rychlik MP]]
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[[Category: Hydrolase-dna-rna hybrid complex]]
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[[Category: Nuclease]]
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[[Category: Rnase h fold]]
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Current revision

T. maritima RNase H2 D107N in complex with nucleic acid substrate and manganese ions

PDB ID 3o3h

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