Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer

Ishchenko, Andrii; Borshchevskiy, Valentin; Grudinin, Sergei; Gushchin, Ivan; Klare, Johann P.; Balandin, Taras; Remeeva, Alina; Engelhard, Martin; Büldt, Georg; Gordeliy, Valentin

doi:10.1016/j.jphotobiol.2013.03.008

Cited by 11 publications

(10 citation statements)

References 28 publications

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“…However, the structure of the NarQ TM domain is notably different from that of the sensory rhodopsin transducer TM domain ( Figure S5). In NarQ, the TM region is either a simple 4helical CC, or has a dimeric CC core consisting of the helices TM1, whereas NpHtrII has a dimeric CC core consisting of the helices TM2 (14,28). Also, in NarQ, there is either zero or left-handed supercoil twist, while in NpHtrII this changes from close to zero at the periplasmic side to right-handed at the cytoplasmic side ( Figure S5).…”

Section: Structure Of the Tm Domainmentioning

confidence: 99%

Mechanism of transmembrane signaling by sensor histidine kinases

Gushchin

Melnikov

Polovinkin

et al. 2017

Science

148

181

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One of the major and essential classes of transmembrane (TM) receptors, present in all domains of life, is sensor histidine kinases, parts of two-component signaling systems (TCSs). The structural mechanisms of TM signaling by these sensors are poorly understood. We present crystal structures of the periplasmic sensor domain, the TM domain, and the cytoplasmic HAMP domain of the nitrate/nitrite sensor histidine kinase NarQ in the ligand-bound and mutated ligand-free states. The structures reveal that the ligand binding induces rearrangements and pistonlike shifts of TM helices. The HAMP domain protomers undergo leverlike motions and convert these pistonlike motions into helical rotations. Our findings provide the structural framework for complete understanding of TM TCS signaling and for development of antimicrobial treatments targeting TCSs.

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Section: Structure Of the Tm Domainmentioning

confidence: 99%

Mechanism of transmembrane signaling by sensor histidine kinases

Gushchin

Melnikov

Polovinkin

et al. 2017

Science

148

181

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“…Light induced conformational changes have been observed for Np SRII and Np HtrII. Upon photo activation Np SRII undergoes an outward motion of helix F [ 7 – 10 ], which induces a clockwise rotation of helix TM2 of Np HtrII along with a displacement [ 8 , 11 , 12 ], presumably similar to the piston-like motion in chemoreceptors [ 13 – 15 ]. These transient changes in the transmembrane part of Np HtrII lead to switching between conformational states of the membrane adjacent HAMP domain [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis

et al. 2015

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Motile bacteria and archaea respond to chemical and physical stimuli seeking optimal conditions for survival. To this end transmembrane chemo- and photoreceptors organized in large arrays initiate signaling cascades and ultimately regulate the rotation of flagellar motors. To unravel the molecular mechanism of signaling in an archaeal phototaxis complex we performed coarse-grained molecular dynamics simulations of a trimer of receptor/transducer dimers, namely NpSRII/NpHtrII from Natronomonas pharaonis. Signaling is regulated by a reversible methylation mechanism called adaptation, which also influences the level of basal receptor activation. Mimicking two extreme methylation states in our simulations we found conformational changes for the transmembrane region of NpSRII/NpHtrII which resemble experimentally observed light-induced changes. Further downstream in the cytoplasmic domain of the transducer the signal propagates via distinct changes in the dynamics of HAMP1, HAMP2, the adaptation domain and the binding region for the kinase CheA, where conformational rearrangements were found to be subtle. Overall these observations suggest a signaling mechanism based on dynamic allostery resembling models previously proposed for E. coli chemoreceptors, indicating similar properties of signal transduction for archaeal photoreceptors and bacterial chemoreceptors.

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“…The third normal mode largely overlaps with the PC1 of PCA analysis. This motional mode is of special interest as it closely resembles the transition between the “U”‐ and “V”‐shaped conformations of the Np SRII: Np HtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process . Indeed, the histogram of the trajectory projection on the PC1 as well as the histograms of the intermonomer SRII‐SRII angle (between helices F) and distance (between the COMs of the cytoplasmic segment of helix F in both monomers) distributions are clearly bimodal indicating the presence of two conformations.…”

Section: Resultsmentioning

confidence: 73%

“…and Figure and Table ). One of these global modes resembles the conformational change (a relative orientation of Np SRII molecules within a dimer reminiscent of the “U”‐”V” shape change), which was previously attributed to the activation process based on the alternative symmetries of the receptor complex revealed by X‐ray crystallography . Such large amplitude global motions, which at the same time are associated with a subtle free energy change, can allosterically spread across the two‐dimensional transmembrane lattice triggering a cooperative activation of multiple copies of the receptors, which can provide an additional level for signal amplification.…”

Section: Discussionmentioning

confidence: 96%

Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers

Orekhov

Bothe

Steinhoff

et al. 2017

Photochem & Photobiology

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Archaeal photoreceptors consist of sensory rhodopsins in complex with their cognate transducers. After light excitation, a two-component signaling chain is activated, which is homologous to the chemotactic signaling cascades in enterobacteria. The latter system has been studied in detail. From structural and functional studies, a picture emerges which includes stable signaling complexes, which assemble to receptor arrays displaying hexagonal structural elements. At this higher order structural level, signal amplification and sensory adaptation occur. Here, we describe electron microscopy data, which show that also the archaeal phototaxis receptors sensory rhodopsin I and II in complex with their cognate transducers can form hexagonal lattices even in the presence of a detergent. This result could be confirmed by molecular dynamics calculations, which revealed similar structural elements. Calculations of the global modes of motion displayed one mode, which resembles the "U"-"V" transition of the NpSRII:NpHtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process [Ishchenko et al. (2013) J. Photochem. Photobiol. B 123, 55-58]. A model of cooperativity at the transmembrane level is discussed.

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Ground state structure of D75N mutant of sensory rhodopsin II in complex with its cognate transducer

Cited by 11 publications

References 28 publications

Mechanism of transmembrane signaling by sensor histidine kinases

Mechanism of transmembrane signaling by sensor histidine kinases

Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonis

Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers

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