5y9p: Difference between revisions
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==Staphylococcus aureus RNase HII== | ==Staphylococcus aureus RNase HII== | ||
<StructureSection load='5y9p' size='340' side='right' caption='[[5y9p]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5y9p' size='340' side='right'caption='[[5y9p]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5y9p]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5y9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y9P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5y9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9p OCA], [https://pdbe.org/5y9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y9p RCSB], [https://www.ebi.ac.uk/pdbsum/5y9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9p ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RNH2_STAA8 RNH2_STAA8] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00052] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5y9p" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5y9p" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Hang T]] | ||
[[Category: | [[Category: Wu M]] | ||
[[Category: | [[Category: Zhang X]] | ||
Latest revision as of 11:25, 22 November 2023
Staphylococcus aureus RNase HIIStaphylococcus aureus RNase HII
Structural highlights
FunctionRNH2_STAA8 Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00052] Publication Abstract from PubMedRNase HII exists ubiquitously in organisms and functions as a monomer in prokaryotes. We determined the crystal structure of Staphylococcus aureus RNase HII (Sa-RNase HII), which displays a novel dimer conformation, with the active site of each monomer covered by the other one. Both small-angle X-ray scattering and gel-filtration analysis confirmed that Sa-RNase HII exists as a homodimer in solution. Enzymatic analysis revealed that the "self-inhibited" dimeric form is catalytically active. Furthermore, continuous-wave electron paramagnetic resonance experiments clarified that the Sa-RNase HII dimer undergoes a large conformational change upon substrate binding, but remains a dimer to catalyze the reaction. Our structural and biochemical studies identified a novel functional dimer of Sa-RNase HII with distinct regulation mechanism for its catalytic activity. Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII.,Hang T, Zhang X, Wu M, Wang C, Ling S, Xu L, Gong Q, Tian C, Zhang X, Zang J Biochem Biophys Res Commun. 2018 Jul 10. pii: S0006-291X(18)31521-3. doi:, 10.1016/j.bbrc.2018.07.026. PMID:30005877[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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