View source for 5y9p


==Staphylococcus aureus RNase HII==
<StructureSection load='5y9p' size='340' side='right'caption='[[5y9p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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></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>
</table>
== 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;">
== Publication Abstract from PubMed ==
RNase 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<ref>PMID:30005877</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5y9p" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Hang T]]
[[Category: Wu M]]
[[Category: Zhang X]]