4gcz
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4gcz is ON HOLD Authors: Diensthuber, R.P., Bommer, M., Moglich, A. Description: Structure of a blue-light photoreceptor) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==Structure of a blue-light photoreceptor== |
| + | <StructureSection load='4gcz' size='340' side='right'caption='[[4gcz]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4gcz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168] and [https://en.wikipedia.org/wiki/Bradyrhizobium_diazoefficiens_USDA_110 Bradyrhizobium diazoefficiens USDA 110]. The March 2015 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phototropin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2015_3 10.2210/rcsb_pdb/mom_2015_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GCZ 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]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4gcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gcz OCA], [https://pdbe.org/4gcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gcz RCSB], [https://www.ebi.ac.uk/pdbsum/4gcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gcz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHOT_BACSU PHOT_BACSU] Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Although it is a positive regulator in the activation of the environmental signaling branch of the general stress transcription factor sigma-B, its precise role is undetermined.<ref>PMID:11157946</ref> [https://www.uniprot.org/uniprot/FIXL_BRADU FIXL_BRADU] Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Two-component systems (TCSs), which comprise sensor histidine kinases (SHK) and response-regulator proteins, represent the predominant strategy by which prokaryotes sense and respond to a changing environment. Despite paramount biological importance, a dearth exists of intact SHK structures containing both sensor and effector modules. Here, we report the full-length crystal structure of the engineered, dimeric, blue-light-regulated SHK YF1 at 2.3 A resolution, in which two N-terminal light-oxygen-voltage (LOV) photosensors are connected by a coiled coil to the C-terminal effector modules. A second coaxial coiled coil derived from the N-termini of the LOV photosensors and inserted between them crucially modulates light regulation: single mutations within this coiled coil attenuate or even invert the signal response of the TCS. Structural motifs identified in YF1 recur in signal receptors, and the underlying signaling principles and mechanisms may be widely shared between soluble and transmembrane, prokaryotic, and eukaryotic signal receptors of diverse biological activity. | ||
| - | + | Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators.,Diensthuber RP, Bommer M, Gleichmann T, Moglich A Structure. 2013 Jul 2;21(7):1127-36. doi: 10.1016/j.str.2013.04.024. Epub 2013, Jun 6. PMID:23746806<ref>PMID:23746806</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4gcz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
| + | [[Category: Bradyrhizobium diazoefficiens USDA 110]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phototropin]] | ||
| + | [[Category: RCSB PDB Molecule of the Month]] | ||
| + | [[Category: Bommer M]] | ||
| + | [[Category: Diensthuber RP]] | ||
| + | [[Category: Moglich A]] | ||
Current revision
Structure of a blue-light photoreceptor
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