2bun: Difference between revisions
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<StructureSection load='2bun' size='340' side='right'caption='[[2bun]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2bun' size='340' side='right'caption='[[2bun]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bun]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2bun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUN FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bun OCA], [https://pdbe.org/2bun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bun RCSB], [https://www.ebi.ac.uk/pdbsum/2bun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bun ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[BLUF domain protein | *[[AppA protein BLUF domain|AppA protein BLUF domain]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:27, 10 November 2021
Solution structure of the BLUF domain of AppA 5-125Solution structure of the BLUF domain of AppA 5-125
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe transcriptional antirepressor AppA from the photosynthetic bacterium Rhodobacter sphaeroides senses both the light climate and the intracellular redox state. Under aerobic conditions in the dark, AppA binds to and thereby blocks the function of PpsR, a transcriptional repressor. Absorption of a blue photon dissociates AppA from PpsR and allows the latter to repress photosynthesis gene expression. The N terminus of AppA contains sequence homology to flavin-containing photoreceptors that belong to the BLUF family. Structural and chemical aspects of signal transduction mediated by AppA are still largely unknown. Here we present NMR studies of the N-terminal flavin-binding BLUF domain of AppA. Its solution structure adopts an alpha/beta-sandwich fold with a beta alpha beta beta alpha beta beta topology, which represents a new flavin-binding fold. Considerable disorder is observed for residues near the chromophore due to conformational exchange. This disorder is observed both in the dark and in the light-induced signaling state of AppA. Furthermore, we detect light-induced structural changes in a patch of surface residues that provide a structural link between light absorption and signal-transduction events. The solution structure of the AppA BLUF domain: insight into the mechanism of light-induced signaling.,Grinstead JS, Hsu ST, Laan W, Bonvin AM, Hellingwerf KJ, Boelens R, Kaptein R Chembiochem. 2006 Jan;7(1):187-93. PMID:16323221[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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