6nx0: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the diheme peroxidase BthA from Burkholderia thailandensis E264== | |||
<StructureSection load='6nx0' size='340' side='right'caption='[[6nx0]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6nx0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_thailandensis_E264 Burkholderia thailandensis E264]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6NX0 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]] 1.54Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=6nx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nx0 OCA], [https://pdbe.org/6nx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nx0 RCSB], [https://www.ebi.ac.uk/pdbsum/6nx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nx0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2T6B0_BURTA Q2T6B0_BURTA] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6nx0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome c peroxidase 3D structures|Cytochrome c peroxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Burkholderia thailandensis E264]] | |||
[[Category: Large Structures]] | |||
[[Category: Cohen SE]] | |||
[[Category: Drennan CL]] | |||
Latest revision as of 07:01, 11 October 2023
Crystal structure of the diheme peroxidase BthA from Burkholderia thailandensis E264
| ||||||||||||
