5y9p: Difference between revisions
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==Staphylococcus aureus RNase HII== | |||
<StructureSection load='5y9p' size='340' side='right' caption='[[5y9p]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5y9p]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9P 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></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9p OCA], [http://pdbe.org/5y9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9p RCSB], [http://www.ebi.ac.uk/pdbsum/5y9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A0D6HS53_STAAU A0A0D6HS53_STAAU]] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00052][RuleBase:RU003515][SAAS:SAAS00946624] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5y9p" style="background-color:#fffaf0;"></div> | ||
[[Category: Wu, M | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ribonuclease H]] | |||
[[Category: Hang, T]] | |||
[[Category: Wu, M]] | |||
[[Category: Zhang, X]] | |||
[[Category: Endonuclease]] | |||
[[Category: Hydrolase]] | |||
Revision as of 21:38, 1 August 2018
Staphylococcus aureus RNase HIIStaphylococcus aureus RNase HII
Structural highlights
Function[A0A0D6HS53_STAAU] Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.[HAMAP-Rule:MF_00052][RuleBase:RU003515][SAAS:SAAS00946624] 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. References
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