5LLX
Bacteriophytochrome activated diguanylyl cyclase from Idiomarina species A28L with GTP bound
Summary for 5LLX
| Entry DOI | 10.2210/pdb5llx/pdb |
| Descriptor | Diguanylate cyclase (GGDEF) domain-containing protein, 3-[2-[(Z)-[3-(2-carboxyethyl)-5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-4-methyl-pyrrol-1-ium -2-ylidene]methyl]-5-[(Z)-[(3E)-3-ethylidene-4-methyl-5-oxidanylidene-pyrrolidin-2-ylidene]methyl]-4-methyl-1H-pyrrol-3- yl]propanoic acid, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | bacteriophytochrome, diguanylate cyclase, light-regulation, gtp, soak, transferase |
| Biological source | Idiomarina sp. A28L |
| Total number of polymer chains | 2 |
| Total formula weight | 158657.78 |
| Authors | Gourinchas, G.,Winkler, A. (deposition date: 2016-07-28, release date: 2017-03-15, Last modification date: 2024-10-23) |
| Primary citation | Gourinchas, G.,Etzl, S.,Gobl, C.,Vide, U.,Madl, T.,Winkler, A. Long-range allosteric signaling in red light-regulated diguanylyl cyclases. Sci Adv, 3:e1602498-e1602498, 2017 Cited by PubMed Abstract: Nature has evolved an astonishingly modular architecture of covalently linked protein domains with diverse functionalities to enable complex cellular networks that are critical for cell survival. The coupling of sensory modules with enzymatic effectors allows direct allosteric regulation of cellular signaling molecules in response to diverse stimuli. We present molecular details of red light-sensing bacteriophytochromes linked to cyclic dimeric guanosine monophosphate-producing diguanylyl cyclases. Elucidation of the first crystal structure of a full-length phytochrome with its enzymatic effector, in combination with the characterization of light-induced changes in conformational dynamics, reveals how allosteric light regulation is fine-tuned by the architecture and composition of the coiled-coil sensor-effector linker and also the central helical spine. We anticipate that consideration of molecular principles of sensor-effector coupling, going beyond the length of the characteristic linker, and the appreciation of dynamically driven allostery will open up new directions for the design of novel red light-regulated optogenetic tools. PubMed: 28275738DOI: 10.1126/sciadv.1602498 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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