6pl0 | pdb_00006pl0
Crystal structure of the dark-adapted full-length bacteriophytochrome XccBphP from Xanthomonas campestris in the Pr state bound to BV chromophore
Structural highlights
FunctionBPHY_XANC8 Photoreceptor which exists in two forms that are reversibly interconvertible by light: far-red light (733 nm) converts protein to the red-absorbing (Pr) form, while red light (630 nm) partly converts the protein to the far-red-absorbing (Pfr) form (PubMed:27107635). Regulates virulence of X.campestris pv. campestris on its host plants, perhaps by fine-tuning expression to ambient light levels and/or spatial cues (PubMed:27621284). The Pr form may sense light and partially inhibit virulence; in the dark (Pfr form) biofilm and xanathan production rise and bacteria are more virulent (PubMed:27621284). Strains overexpressing this protein have significantly decreased amounts of extracellular beta-1,4-endoglucanase, produce less xanthin and have decreased transcription of genes involved in virulence such as endoglucanases, type 2 secretion systems, xanthan production and flagellar-dependent motility (PubMed:27621284).[1] [2] [3] Publication Abstract from PubMed[Figure: see text]. Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level.,Otero LH, Foscaldi S, Antelo GT, Rosano GL, Sirigu S, Klinke S, Defelipe LA, Sanchez-Lamas M, Battocchio G, Conforte V, Vojnov AA, Chavas LMG, Goldbaum FA, Mroginski MA, Rinaldi J, Bonomi HR Sci Adv. 2021 Nov 26;7(48):eabh1097. doi: 10.1126/sciadv.abh1097. Epub 2021 Nov, 24. PMID:34818032[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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