View source for 6xvu


==Bacteriophytochrome response regulator from Deinococcus radiodurans==
<StructureSection load='6xvu' size='340' side='right'caption='[[6xvu]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xvu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XVU 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6xvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xvu OCA], [https://pdbe.org/6xvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xvu RCSB], [https://www.ebi.ac.uk/pdbsum/6xvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xvu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9RZA5_DEIRA Q9RZA5_DEIRA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial phytochrome photoreceptors usually belong to two-component signaling systems which transmit environmental stimuli to a response regulator through a histidine kinase domain. Phytochromes switch between red light-absorbing and far-red light-absorbing states. Despite exhibiting extensive structural responses during this transition, the model bacteriophytochrome from Deinococcus radiodurans (DrBphP) lacks detectable kinase activity. Here, we resolve this long-standing conundrum by comparatively analyzing the interactions and output activities of DrBphP and a bacteriophytochrome from Agrobacterium fabrum (Agp1). Whereas Agp1 acts as a conventional histidine kinase, we identify DrBphP as a light-sensitive phosphatase. While Agp1 binds its cognate response regulator only transiently, DrBphP does so strongly, which is rationalized at the structural level. Our data pinpoint two key residues affecting the balance between kinase and phosphatase activities, which immediately bears on photoreception and two-component signaling. The opposing output activities in two highly similar bacteriophytochromes suggest the use of light-controllable histidine kinases and phosphatases for optogenetics.

Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling.,Multamaki E, Nanekar R, Morozov D, Lievonen T, Golonka D, Wahlgren WY, Stucki-Buchli B, Rossi J, Hytonen VP, Westenhoff S, Ihalainen JA, Moglich A, Takala H Nat Commun. 2021 Jul 20;12(1):4394. doi: 10.1038/s41467-021-24676-7. PMID:34285211<ref>PMID:34285211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xvu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: Ihalainen JA]]
[[Category: Takala H]]