4KUK
A superfast recovering full-length LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae (Dark state)
Summary for 4KUK
| Entry DOI | 10.2210/pdb4kuk/pdb |
| Related | 4KUO |
| Descriptor | blue-light photoreceptor, RIBOFLAVIN, ACETIC ACID, ... (4 entities in total) |
| Functional Keywords | pas domain, light-oxygen-voltage, lov, fmn binding, signaling protein |
| Biological source | Dinoroseobacter shibae |
| Total number of polymer chains | 1 |
| Total formula weight | 17310.35 |
| Authors | Circolone, F.,Granzin, J.,Stadler, A.,Krauss, U.,Drepper, T.,Endres, S.,Knieps-Gruenhagen, E.,Wirtz, A.,Willbold, D.,Batra-Safferling, R.,Jaeger, K.-E. (deposition date: 2013-05-22, release date: 2014-11-26, Last modification date: 2023-09-20) |
| Primary citation | Endres, S.,Granzin, J.,Circolone, F.,Stadler, A.,Krauss, U.,Drepper, T.,Svensson, V.,Knieps-Grunhagen, E.,Wirtz, A.,Cousin, A.,Tielen, P.,Willbold, D.,Jaeger, K.E.,Batra-Safferling, R. Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae. BMC Microbiol, 15:30-30, 2015 Cited by PubMed Abstract: Light, oxygen, voltage (LOV) domains are widely distributed in plants, algae, fungi, bacteria, and represent the photo-responsive domains of various blue-light photoreceptor proteins. Their photocycle involves the blue-light triggered adduct formation between the C(4a) atom of a non-covalently bound flavin chromophore and the sulfur atom of a conserved cysteine in the LOV sensor domain. LOV proteins show considerable variation in the structure of N- and C-terminal elements which flank the LOV core domain, as well as in the lifetime of the adduct state. PubMed: 25887755DOI: 10.1186/s12866-015-0365-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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