View source for 7qbk


==Crystal structure of a second homolog of R2-like ligand-binding oxidase in Sulfolobus acidocaldarius (SaR2loxII)==
<StructureSection load='7qbk' size='340' side='right'caption='[[7qbk]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qbk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius_DSM_639 Sulfolobus acidocaldarius DSM 639]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QBK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QBK 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]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN3:MANGANESE+(III)+ION'>MN3</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=7qbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qbk OCA], [https://pdbe.org/7qbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qbk RCSB], [https://www.ebi.ac.uk/pdbsum/7qbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qbk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q4J9R6_SULAC Q4J9R6_SULAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
R2-like ligand-binding oxidase (R2lox) is a ferritin-like protein that harbours a heterodinuclear manganese-iron active site. Although R2lox function is yet to be established, the enzyme binds a fatty acid ligand coordinating the metal centre and catalyses the formation of a tyrosine-valine ether cross-link in the protein scaffold upon O2 activation. Here, we characterized the ligands copurified with R2lox by mass spectrometry-based metabolomics. Moreover, we present the crystal structures of two new homologs of R2lox, from Saccharopolyspora erythraea and Sulfolobus acidocaldarius, at 1.38 A and 2.26 A resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.

Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase.,Diamanti R, Srinivas V, Johansson AI, Nordstrom A, Griese JJ, Lebrette H, Hogbom M FEBS Lett. 2022 Feb 17. doi: 10.1002/1873-3468.14319. PMID:35175627<ref>PMID:35175627</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qbk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus acidocaldarius DSM 639]]
[[Category: Diamanti R]]
[[Category: Hogbom M]]
[[Category: Lebrette H]]
[[Category: Srinivas V]]