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4py5
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4py5 is ON HOLD Authors: Figiel, M., Nowotny, M. Description: Protein-nucleic acid complex) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Thermovibrio ammonificans RNase H3 in complex with 19-mer RNA/DNA== | |
| + | <StructureSection load='4py5' size='340' side='right'caption='[[4py5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4py5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermovibrio_ammonificans_HB-1 Thermovibrio ammonificans HB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PY5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4py5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4py5 OCA], [https://pdbe.org/4py5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4py5 RCSB], [https://www.ebi.ac.uk/pdbsum/4py5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4py5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/E8T217_THEA1 E8T217_THEA1] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (By similarity).[RuleBase:RU003515][SAAS:SAAS004641_004_003953] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RNases H participate in the replication and maintenance of genomic DNA. RNase H1 cleaves the RNA strand of RNA/DNA hybrids, and RNase H2 in addition hydrolyzes the RNA residue of RNA-DNA junctions. RNase H3 is structurally closely related to RNases H2, but its biochemical properties are similar to type 1 enzymes. Its unique N-terminal substrate-binding domain (N-domain) is related to TATA-binding protein. Here, we report the first crystal structure of RNase H3 in complex with its RNA/DNA substrate. Just like RNases H1, type 3 enzyme recognizes the 2'-OH groups of the RNA strand and detects the DNA strand by binding a phosphate group and inducing B-form conformation. Moreover, the N-domain recognizes RNA and DNA in a manner that is highly similar to the hybrid-binding domain of RNases H1. Our structure demonstrates a remarkable example of parallel evolution of the elements used in the specific recognition of RNA and DNA. | ||
| - | + | Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition.,Figiel M, Nowotny M Nucleic Acids Res. 2014 Jul 12. pii: gku615. PMID:25016521<ref>PMID:25016521</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4py5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermovibrio ammonificans HB-1]] | ||
| + | [[Category: Figiel M]] | ||
| + | [[Category: Nowotny M]] | ||
Current revision
Thermovibrio ammonificans RNase H3 in complex with 19-mer RNA/DNA
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