3D1500 FTIR spectroscopy of the complex between pharaonis phoborhodopsin and its transducer

Furutani, Yuji; Sudo, Yuki; Kamo, N.; Kandori, Hideki

doi:10.2142/biophys.42.s156_2

Cited by 12 publications

(25 citation statements)

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“…Nonetheless we are able to make a conclusion, that there are no changes in the uncomplexed NpSRII active state in the relative positions of the residues T204 and Y174 (Figure 3), which are proposed to be important for the signal generation in NpSRII/NpHtrII complex 42,43 . Probably, this reflects the spectroscopically observed absence of the alteration in T204-Y174 bonding in uncomplexed NpSRII 44,45 .…”

Section: Functionally Important Conformational Changes In Npsriimentioning

confidence: 80%

Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping

Gushchin

Reshetnyak

Borshchevskiy

et al. 2011

Journal of Molecular Biology

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The molecular mechanism of transmembrane signal transduction is still a pertinent question in cellular biology. Generally, a receptor can transfer an external signal via its cytoplasmic surface as found for GPCRs like rhodopsin or via the membrane domain like it is utilized by sensory rhodopsin II (SRII) in complex with its transducer HtrII. In the absence of HtrII SRII functions as a proton pump. Here, we report on the crystal structure of the active state of SRII from Natronomonas pharaonis (NpSRII). The problem of a dramatic loss of the diffraction quality upon loading of the active state was overcome by growing better crystals and reducing the occupancy of the state. The determined conformational changes at the region comprising helices F and G are similar to those observed for the NpSRII-transducer complex but they are much more pronounced. Meaning of these differences for proton pumping ability and understanding of the signal transduction by NpSRII is discussed.

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Section: Functionally Important Conformational Changes In Npsriimentioning

confidence: 80%

Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping

Gushchin

Reshetnyak

Borshchevskiy

et al. 2011

Journal of Molecular Biology

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“…Figure 18.9 shows two exceptions. The 13-cis form of BR [59] and the SRII complex with the transducer protein [60] possess strongly hydrogen-bonded water but no proton-pump activity. However, the former has the 13-cis chromophore, and it is known that only the all-trans chromophore has proton-pump activity.…”

Section: Strongly Hydrogen-bonded Water Molecules and Functional Corrmentioning

confidence: 99%

Hydrogen Bonds of Protein‐Bound Water Molecules in Rhodopsins

Kandori

2010

Hydrogen Bonding and Transfer in the Excited State

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“…The peak at 1671 cm ÿ1 (H 2 O) has a slight shift to lower wavenumbers (1670 cm ÿ1 ). Therefore, this peak may correspond to nonaccessible helix a II (44) or to nonaccessible reverse turns (45). (Fig.…”

Section: Degree Of H/d Exchangementioning

confidence: 99%

Changes in Secondary Structures and Acidic Side Chains of Melibiose Permease upon Cosubstrates Binding

León

Lemonnier

Leblanc

et al. 2006

Biophysical Journal

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Infrared difference spectroscopy analysis of the purified melibiose permease of Escherichia coli reconstituted into liposomes was carried out as a function of the presence of the two symporter substrates (Na(+), melibiose) in either H(2)O or in D(2)O media. Essentially, the data first show that addition of Na(+) induces appearance of peaks assigned to changes in the environment and/or orientation of alpha-helical domains of purified melibiose permease. Likewise, melibiose addition in the presence of Na(+) produces peaks corresponding to additional changes of alpha-helix environment or tilt. In addition to these changes, a pair of peaks (1599 (+) cm(-1)/1576 (-) cm(-1)) appearing in the Na(+)-induced difference spectrum is assigned to the antisymmetric stretching of COO(-) groups, since they show practically no shift upon H/D exchange. It is proposed that these acidic groups participate in Na(+) co-ordination. A corresponding pair of peaks, again fairly insensitive to H/D substitution (1591 (-) cm(-1)/1567 (+) cm(-1)), appear in the melibiose-induced difference spectra, and may again be assigned to COO(-) groups. The latter carboxyl groups may correspond to part or all of the acidic residues interacting with Lys or Arg in the resting state that become free upon melibiose binding.

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3D1500 FTIR spectroscopy of the complex between pharaonis phoborhodopsin and its transducer

Cited by 12 publications

References 0 publications

Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping

Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping

Hydrogen Bonds of Protein‐Bound Water Molecules in Rhodopsins

Changes in Secondary Structures and Acidic Side Chains of Melibiose Permease upon Cosubstrates Binding

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