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5j4e

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<table><tr><td colspan='2'>[[5j4e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J4E FirstGlance]. <br>
<table><tr><td colspan='2'>[[5j4e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J4E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4e OCA], [http://pdbe.org/5j4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j4e RCSB], [http://www.ebi.ac.uk/pdbsum/5j4e PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5j4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j4e OCA], [http://pdbe.org/5j4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j4e RCSB], [http://www.ebi.ac.uk/pdbsum/5j4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j4e ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Light-Oxygen-Voltage (LOV) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi, and bacteria. Here, we report the dark-state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida that is remarkably different from our previously published "fully light-adapted" structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a~11A movement of the C terminus in helix Jalpha, ~4A movement of Hbeta-Ibeta loop, disruption of hydrogen bonds in the dimer interface, and a~29 degrees rotation of chain-B relative to chain-A as compared to the light-state dimer. Both crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A'alpha-Abeta loop and the A'alpha helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based, two-component systems and regulators.
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Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy.,Rollen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R J Mol Biol. 2016 Jun 9. pii: S0022-2836(16)30206-6. doi:, 10.1016/j.jmb.2016.05.027. PMID:27291287<ref>PMID:27291287</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5j4e" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 18:37, 12 July 2016

Crystal structures reveal signaling states of a short blue light photoreceptor protein PpSB1-LOV (Photoexcited state)

5j4e, resolution 2.67Å

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