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5LLW

Bacteriophytochrome activated diguanylyl cyclase from Idiomarina species A28L

Summary for 5LLW
Entry DOI10.2210/pdb5llw/pdb
DescriptorDiguanylate 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 (3 entities in total)
Functional Keywordsbacteriophytochrome, diguanylate cyclase, light-regulation, c-di-gmp, gtp, hydrolase, transferase
Biological sourceIdiomarina sp. A28L
Total number of polymer chains2
Total formula weight159157.28
Authors
Gourinchas, G.,Winkler, A. (deposition date: 2016-07-28, release date: 2017-03-15, Last modification date: 2024-10-16)
Primary citationGourinchas, 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: 28275738
DOI: 10.1126/sciadv.1602498
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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数据于2024-11-13公开中

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