6nx0: Difference between revisions

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'''Unreleased structure'''


The entry 6nx0 is ON HOLD  until Paper Publication
==Crystal structure of the diheme peroxidase BthA from Burkholderia thailandensis E264==
<StructureSection load='6nx0' size='340' side='right'caption='[[6nx0]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nx0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NX0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=6nx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nx0 OCA], [http://pdbe.org/6nx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nx0 RCSB], [http://www.ebi.ac.uk/pdbsum/6nx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nx0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H2O2) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme peroxidase BthA conserved in all Burkholderia. Using a combination of magnetic resonance, near-IR and Mossbauer spectroscopies and electrochemical methods, we report that BthA is capable of generating a bis-Fe(IV) species previously thought to be a unique feature of the diheme enzyme MauG. However, BthA is not MauG-like in that it catalytically converts H2O2 to water, and a 1.54-A resolution crystal structure reveals striking differences between BthA and other superfamily members, including the essential residues for both bis-Fe(IV) formation and H2O2 turnover. Taken together, we find that BthA represents a previously undiscovered class of diheme enzymes, one that stabilizes a bis-Fe(IV) state and catalyzes H2O2 turnover in a mechanistically distinct manner.


Authors:  
A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.,Rizzolo K, Cohen SE, Weitz AC, Lopez Munoz MM, Hendrich MP, Drennan CL, Elliott SJ Nat Commun. 2019 Mar 7;10(1):1101. doi: 10.1038/s41467-019-09020-4. PMID:30846684<ref>PMID:30846684</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6nx0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cohen, S E]]
[[Category: Drennan, C L]]
[[Category: Diheme]]
[[Category: Heme]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
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