Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR

Tadashi Arakawa, Kazumi Shimono, Satoru Yamaguchi, Satoru Tuzi, Yuki Sudo, Naoki Kamo, Hazime Saitô

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

We have recorded 13C nuclear magnetic resonance (NMR) spectra of [3-13C]Ala, [1-13C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven 13C NMR signals from transmembrane α-helices were resolved for [3-13C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, 13C NMR signals from the loops were visible from [1-13C]Val-ppR but their peak positions of the transmembrane α-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 105 Hz in view of the suppressed peaks from [3-13C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1-159). In particular, the C-terminal α-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude.

Original languageEnglish
Pages (from-to)237-240
Number of pages4
JournalFEBS Letters
Volume536
Issue number1-3
DOIs
Publication statusPublished - Feb 11 2003
Externally publishedYes

Fingerprint

Sensory Rhodopsins
Transducers
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Bacteriorhodopsins
Phosphatidylcholines
Ovum
Conformations
Protons
Membranes

Keywords

  • Cognate transducer
  • Conformation and dynamics
  • Membrane protein
  • Pharaonis phoborhodopsin
  • Sensory rhodopsin II
  • Site-directed C solid-state NMR

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR. / Arakawa, Tadashi; Shimono, Kazumi; Yamaguchi, Satoru; Tuzi, Satoru; Sudo, Yuki; Kamo, Naoki; Saitô, Hazime.

In: FEBS Letters, Vol. 536, No. 1-3, 11.02.2003, p. 237-240.

Research output: Contribution to journalArticle

Arakawa, Tadashi ; Shimono, Kazumi ; Yamaguchi, Satoru ; Tuzi, Satoru ; Sudo, Yuki ; Kamo, Naoki ; Saitô, Hazime. / Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR. In: FEBS Letters. 2003 ; Vol. 536, No. 1-3. pp. 237-240.
@article{78a132b61ce04a1f9de066972ebacbce,
title = "Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR",
abstract = "We have recorded 13C nuclear magnetic resonance (NMR) spectra of [3-13C]Ala, [1-13C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven 13C NMR signals from transmembrane α-helices were resolved for [3-13C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, 13C NMR signals from the loops were visible from [1-13C]Val-ppR but their peak positions of the transmembrane α-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 105 Hz in view of the suppressed peaks from [3-13C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1-159). In particular, the C-terminal α-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude.",
keywords = "Cognate transducer, Conformation and dynamics, Membrane protein, Pharaonis phoborhodopsin, Sensory rhodopsin II, Site-directed C solid-state NMR",
author = "Tadashi Arakawa and Kazumi Shimono and Satoru Yamaguchi and Satoru Tuzi and Yuki Sudo and Naoki Kamo and Hazime Sait{\^o}",
year = "2003",
month = "2",
day = "11",
doi = "10.1016/S0014-5793(03)00065-6",
language = "English",
volume = "536",
pages = "237--240",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1-3",

}

TY - JOUR

T1 - Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR

AU - Arakawa, Tadashi

AU - Shimono, Kazumi

AU - Yamaguchi, Satoru

AU - Tuzi, Satoru

AU - Sudo, Yuki

AU - Kamo, Naoki

AU - Saitô, Hazime

PY - 2003/2/11

Y1 - 2003/2/11

N2 - We have recorded 13C nuclear magnetic resonance (NMR) spectra of [3-13C]Ala, [1-13C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven 13C NMR signals from transmembrane α-helices were resolved for [3-13C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, 13C NMR signals from the loops were visible from [1-13C]Val-ppR but their peak positions of the transmembrane α-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 105 Hz in view of the suppressed peaks from [3-13C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1-159). In particular, the C-terminal α-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude.

AB - We have recorded 13C nuclear magnetic resonance (NMR) spectra of [3-13C]Ala, [1-13C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven 13C NMR signals from transmembrane α-helices were resolved for [3-13C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, 13C NMR signals from the loops were visible from [1-13C]Val-ppR but their peak positions of the transmembrane α-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 105 Hz in view of the suppressed peaks from [3-13C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1-159). In particular, the C-terminal α-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude.

KW - Cognate transducer

KW - Conformation and dynamics

KW - Membrane protein

KW - Pharaonis phoborhodopsin

KW - Sensory rhodopsin II

KW - Site-directed C solid-state NMR

UR - http://www.scopus.com/inward/record.url?scp=0037432194&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037432194&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)00065-6

DO - 10.1016/S0014-5793(03)00065-6

M3 - Article

C2 - 12586370

AN - SCOPUS:0037432194

VL - 536

SP - 237

EP - 240

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-3

ER -