Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution

被引:532
作者
Luecke, H [1 ]
Richter, HT
Lanyi, JK
机构
[1] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA
[2] Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA
关键词
D O I
10.1126/science.280.5371.1934
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Photoisomerization of the retinal of bacteriorhodopsin initiates a cyclic reaction in which a proton is translocated across the membrane. Studies of this protein promise a better understanding of how ion pumps function. Together with a large amount of spectroscopic and mutational data, the atomic structure of bacteriorhodopsin, determined in the last decade at increasing resolutions, has suggested plausible but often contradictory mechanisms. X-ray diffraction of bacteriorhodopsin crystals grown in cubic lipid phase revealed unexpected two-fold symmetries that indicate merohedral twinning along the crystallographic c axis. The structure, refined to 2.3 angstroms taking this twinning into account, is different from earlier models, including that most recently reported. One of the carboxyl oxygen atoms of the proton acceptor Asp(85) is connected to the proton donor, the retinal Schiff base, through a hydrogen-bonded water and forms a second hydrogen bond with another water. The other carboxyl oxygen atom of Asp(85) accepts a hydrogen bond from Thr(89). This structure forms the active site. The nearby Arg(82) is the center of a network of numerous hydrogen-bonded residues and an ordered water molecule. This network defines the pathway of the proton from the buried Schiff base to the extracellular surface.
引用
收藏
页码:1934 / 1937
页数:4
相关论文
共 25 条
  • [1] Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    Balashov, SP
    Imasheva, ES
    Govindjee, R
    Ebrey, TG
    [J]. BIOPHYSICAL JOURNAL, 1996, 70 (01) : 473 - 481
  • [2] EFFECT OF THE ARGININE-82 TO ALANINE MUTATION IN BACTERIORHODOPSIN ON DARK-ADAPTATION, PROTON RELEASE, AND THE PHOTOCHEMICAL CYCLE
    BALASHOV, SP
    GOVINDJEE, R
    KONO, M
    IMASHEVA, E
    LUKASHEV, E
    EBREY, TG
    CROUCH, RK
    MENICK, DR
    FENG, Y
    [J]. BIOCHEMISTRY, 1993, 32 (39) : 10331 - 10343
  • [3] Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    Balashov, SP
    Imasheva, ES
    Ebrey, TG
    Chen, N
    Menick, DR
    Crouch, RK
    [J]. BIOCHEMISTRY, 1997, 36 (29) : 8671 - 8676
  • [4] THE PROTON TRANSFERS IN THE CYTOPLASMIC DOMAIN OF BACTERIORHODOPSIN ARE FACILITATED BY A CLUSTER OF INTERACTING RESIDUES
    BROWN, LS
    YAMAZAKI, Y
    MAEDA, A
    SUN, L
    NEEDLEMAN, R
    LANYI, JK
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1994, 239 (03) : 401 - 414
  • [5] GLUTAMIC-ACID-204 IS THE TERMINAL PROTON RELEASE GROUP AT THE EXTRACELLULAR SURFACE OF BACTERIORHODOPSIN
    BROWN, LS
    SASAKI, J
    KANDORI, H
    MAEDA, A
    NEEDLEMAN, R
    LANYI, JK
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (45) : 27122 - 27126
  • [6] BROWN LS, UNPUB
  • [7] BRUNGER AT, 1992, XPLOR VERSION 3 1 SY
  • [8] NUCLEAR MAGNETIC-RESONANCE STUDY OF THE SCHIFF-BASE IN BACTERIORHODOPSIN - COUNTERION EFFECTS ON THE N-15 SHIFT ANISOTROPY
    DEGROOT, HJM
    HARBISON, GS
    HERZFELD, J
    GRIFFIN, RG
    [J]. BIOCHEMISTRY, 1989, 28 (08) : 3346 - 3353
  • [9] Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    Dioumaev, AK
    Richter, HT
    Brown, LS
    Tanio, M
    Tuzi, S
    Saito, H
    Kimura, Y
    Needleman, R
    Lanyi, JK
    [J]. BIOCHEMISTRY, 1998, 37 (08) : 2496 - 2506
  • [10] Electron-crystallographic refinement of the structure of bacteriorhodopsin
    Grigorieff, N
    Ceska, TA
    Downing, KH
    Baldwin, JM
    Henderson, R
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 259 (03) : 393 - 421