Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome

Woitowich, N.C.; Halavaty, A.S.; Waltz, P.; Kupitz, C.; Valera, J.; Tracy, G.; Gallagher, K.D.; Claesson, E.; Nakane, T.; Pandey, S.; Nelson, G.; Tanaka, R.; Nango, E.; Mizohata, E.; Owada, S.; Tono, K.; Joti, Y.; Nugent, A.C.; Patel, H.; Mapara, A.; Hopkins, J.; Duong, P.; Bizhga, D.; Kovaleva, S.E.; St. Peter, R.; Hernandez, C.N.; Ozarowski, W.B.; Roy-Chowdhuri, S.; Yang, J.-H.; Edlund, P.; Takala, H.; Ihalainen, J.; Brayshaw, J.; Norwood, T.; Poudyal, I.; Fromme, P.; Spence, J.C.H.; Moffat, K.; Westenhoff, S.; Schmidt, M.; Stojkovic, E.A.

doi:10.1107/S2052252518010631

Figure 9
The chromophore and sensory tongue region of the SaBphP1-PCM in the Pr conformation compared with the DrBphP-PCM in the Pfr form. Residues that are considered essential for the Pr to Pfr transition are marked. Red dotted lines: interactions of important residues. (a) Chromophore region of the SaBphP1-PCM, BV ring D is in the Z-configuration. Gray arrow, direction of the structural displacement of P471 from Pr to Pfr. (b) Chromophore region of the DrBphP-PCM F469W mutant (Burgie et al., 2016

), ring D is in the E-configuration. H290 interacts with the ring D propionate. Note, compared with the published structure, the His290 ring was rotated by 180° about the χ² angle to motivate the interaction. The DrBphP residues Ser468, Arg466 and Pro465 correspond to Ser474, Arg472 and Pro471 in SaBphP1, respectively (see also Fig. 4