4py5: Difference between revisions
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<StructureSection load='4py5' size='340' side='right'caption='[[4py5]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4py5' size='340' side='right'caption='[[4py5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4py5]] is a 3 chain structure with sequence from [ | <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"><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='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=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'>[ | <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> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermovibrio ammonificans HB-1]] | ||
[[Category: Figiel | [[Category: Figiel M]] | ||
[[Category: Nowotny | [[Category: Nowotny M]] | ||
Latest revision as of 06:26, 21 November 2024
Thermovibrio ammonificans RNase H3 in complex with 19-mer RNA/DNAThermovibrio ammonificans RNase H3 in complex with 19-mer RNA/DNA
Structural highlights
Publication Abstract from PubMedRNases 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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