View source for 6r9n


==Peroxy diiron species of chemotaxis sensor ODP==
<StructureSection load='6r9n' size='340' side='right'caption='[[6r9n]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6r9n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_denticola_ATCC_35404 Treponema denticola ATCC 35404]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R9N 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]] 2.074&#8491;</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=PER:PEROXIDE+ION'>PER</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=6r9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r9n OCA], [https://pdbe.org/6r9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r9n RCSB], [https://www.ebi.ac.uk/pdbsum/6r9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r9n ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many bacteria contain cytoplasmic chemoreceptors that lack sensor domains. Here, we demonstrate that such cytoplasmic receptors found in 8 different bacterial and archaeal phyla genetically couple to metalloproteins related to beta-lactamases and nitric oxide reductases. We show that this oxygen-binding di-iron protein (ODP) acts as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable mu-peroxo adduct. Crystal structures of ODP from Td and the thermophile Thermotoga maritima (Tm) in the Fe[III]2-O2 (2-), Zn[II], and apo states display differences in subunit association, conformation, and metal coordination that indicate potential mechanisms for sensing. In reconstituted systems, iron-peroxo ODP destabilizes the phosphorylated form of the receptor-coupled histidine kinase CheA, thereby providing a biochemical link between oxygen sensing and chemotaxis in diverse prokaryotes, including anaerobes of ancient origin.

A di-iron protein recruited as an Fe[II] and oxygen sensor for bacterial chemotaxis functions by stabilizing an iron-peroxy species.,Muok AR, Deng Y, Gumerov VM, Chong JE, DeRosa JR, Kurniyati K, Coleman RE, Lancaster KM, Li C, Zhulin IB, Crane BR Proc Natl Acad Sci U S A. 2019 Jul 3. pii: 1904234116. doi:, 10.1073/pnas.1904234116. PMID:31270241<ref>PMID:31270241</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6r9n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Treponema denticola ATCC 35404]]
[[Category: Crane BR]]
[[Category: Muok AR]]