View source for 4nrn


==Crystal structure of metal-bound toxin from Helicobacter pylori==
<StructureSection load='4nrn' size='340' side='right'caption='[[4nrn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4nrn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NRN 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]] 1.802&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4nrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nrn OCA], [https://pdbe.org/4nrn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nrn RCSB], [https://www.ebi.ac.uk/pdbsum/4nrn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nrn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O25552_HELPY O25552_HELPY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Antibiotic resistance and microorganism virulence have been consistently exhibited by bacteria and archaea, which survive in conditions of environmental stress through toxin-antitoxin (TA) systems. The HP0892-HP0893 TA system is one of the two known TA systems belonging to Helicobacter pylori. The antitoxin, HP0893, binds and inhibits the HP0892 toxin and regulates the transcription of the TA operon. Here, we present the crystal structure of the zinc-bound HP0892 toxin at 1.8 A resolution. Reorientation of residues at the mRNase active site was shown. The involved residues, namely E58A, H86A, and H58A/ H60A, were mutated and the binding affinity was monitored by ITC studies. Through the structural difference between the apo and the metal-bound state, and using a homology modeling tool, the involvement of the metal ion in mRNase active site could be identified. The most catalytically important residue, His86, reorients itself to exhibit RNase activity. His47, Glu58, and His60 are involved in metal binding where Glu58 acts as a general base and His47 and His60 may also act as a general acid in enzymatic activity. Glu58 and Asp64 are involved in substrate binding and specific sequence recognition. Arg83 is involved in phosphate binding and stabilization of the transition state, and Phe90 is involved in base packing and substrate orientation.

Crystal structure of toxin HP0892 from Helicobacter pylori with two Zn(II) at 1.8 A resolution.,Im H, Jang SB, Pathak C, Yang YJ, Yoon HJ, Yu TK, Suh JY, Lee BJ Protein Sci. 2014 Jun;23(6):819-32. doi: 10.1002/pro.2465. Epub 2014 Apr 15. PMID:24677509<ref>PMID:24677509</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4nrn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Im H]]
[[Category: Jang SB]]
[[Category: Lee BJ]]
[[Category: Pathak C]]