8uph
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Prf state of Stigmatella aurantiaca bacteriophytochrome 2== | |
| + | <StructureSection load='8uph' size='340' side='right'caption='[[8uph]], [[Resolution|resolution]] 4.13Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8uph]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stigmatella_aurantiaca Stigmatella aurantiaca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UPH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.13Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</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=8uph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8uph OCA], [https://pdbe.org/8uph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8uph RCSB], [https://www.ebi.ac.uk/pdbsum/8uph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8uph ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1H7ZJA8_STIAU A0A1H7ZJA8_STIAU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phytochromes are red-light photoreceptors discovered in plants with homologs in bacteria and fungi that regulate a variety of physiological responses. They display a reversible photocycle between two distinct states: a red-light-absorbing Pr state and a far-red light-absorbing Pfr state. The photoconversion regulates the activity of an enzymatic domain, usually a histidine kinase (HK). The molecular mechanism that explains how light controls the HK activity is not understood because structures of unmodified bacterial phytochromes with HK activity are missing. Here, we report three cryo-electron microscopy structures of a wild-type bacterial phytochrome with HK activity determined as Pr and Pfr homodimers and as a Pr/Pfr heterodimer with individual subunits in distinct states. We propose that the Pr/Pfr heterodimer is a physiologically relevant signal transduction intermediate. Our results offer insight into the molecular mechanism that controls the enzymatic activity of the HK as part of a bacterial two-component system that perceives and transduces light signals. | ||
| - | + | Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM.,Malla TN, Hernandez C, Muniyappan S, Menendez D, Bizhga D, Mendez JH, Schwander P, Stojkovic EA, Schmidt M Sci Adv. 2024 Aug 9;10(32):eadq0653. doi: 10.1126/sciadv.adq0653. Epub 2024 Aug , 9. PMID:39121216<ref>PMID:39121216</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8uph" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Stigmatella aurantiaca]] | ||
| + | [[Category: Malla TN]] | ||
| + | [[Category: Schmidt M]] | ||
| + | [[Category: Stojkovic EA]] | ||
Current revision
Prf state of Stigmatella aurantiaca bacteriophytochrome 2
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