An eye lens protein-water structure: 1.2 angstrom resolution structure of gamma B-crystallin at 150K

被引:57
作者
Kumaraswamy, VS
Lindley, PF
Slingsby, C
Glover, ID
机构
[1] CCLRC, DARESBURY LAB, WARRINGTON WA4 4AD, CHESHIRE, ENGLAND
[2] UNIV LONDON BIRKBECK COLL, DEPT CRYSTALLOG, LONDON WC1E 7HX, ENGLAND
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1996年 / 52卷
关键词
D O I
10.1107/S0907444995014302
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
gamma B-crystallin is a structural protein of the eye lens with a role in the maintenance of an even distribution of protein and water over distances around the wavelength of light, preserving lens transparency. The structure of the 174-residue bovine protein has already been determined at room temperature to 1.47 Angstrom resolution. By flash freezing the protein crystals, data have now been collected to a nominal resolution limit of 1.2 Angstrom as radiation damage was essentially eliminated. The protein-water model has been refined against this data using the program RESTRAIN converging to an R factor of 18.5% with all data. Atomic positions are clearly indicated in the electron-density maps. Discrete bimodal disorder has been visualized for a few side chains. Out of a total of 498 water molecules present in the crystal asymmetric unit, 394 have been modelled and refined at unit occupancy. The solvent structure is extremely well ordered with an average B value of 23.4 Angstrom(2). Partially occupied sites have been identified where disorder in the protein induces concomitant disorder in the local solvent structure. The solvent structure covers 97% of the solvent-exposed surface of the protein in the crystal. 126 water molecules are distributed in second and higher hydration shells. There are networks of hydrogen-bonded solvent extending up to 64 molecules in a network, comprising trimers and tetramers as well as five- and six-membered water-ring structures. The hydration of the protein surface is dominated by arginine and aspartate side chains. Extensive cages of highly ordered solvent molecules are also observed around exposed non-polar groups.
引用
收藏
页码:611 / 622
页数:12
相关论文
共 46 条
  • [1] [Anonymous], ACTA CRYSTALLOGR D
  • [2] ION-PAIRS IN PROTEINS
    BARLOW, DJ
    THORNTON, JM
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1983, 168 (04) : 867 - 885
  • [3] X-RAY-ANALYSIS OF BETA-B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS
    BAX, B
    LAPATTO, R
    NALINI, V
    DRIESSEN, H
    LINDLEY, PF
    MAHADEVAN, D
    BLUNDELL, TL
    SLINGSBY, C
    [J]. NATURE, 1990, 347 (6295) : 776 - 780
  • [4] LIGHT-SCATTERING AND REVERSIBLE CATARACTS IN THE CALF AND HUMAN LENS
    BENEDEK, GB
    CLARK, JI
    SERRALLACH, EN
    YOUNG, CY
    MENGEL, L
    SAUKE, T
    BAGG, A
    BENEDEK, K
    [J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES, 1979, 293 (1402): : 329 - +
  • [5] BLOEMENDAL H, 1991, PROG NUCLEIC ACID RE, V41, P259
  • [6] THE MOLECULAR-STRUCTURE AND STABILITY OF THE EYE LENS - X-RAY-ANALYSIS OF GAMMA-CRYSTALLIN-II
    BLUNDELL, T
    LINDLEY, P
    MILLER, L
    MOSS, D
    SLINGSBY, C
    TICKLE, I
    TURNELL, B
    WISTOW, G
    [J]. NATURE, 1981, 289 (5800) : 771 - 777
  • [7] BLUNDELL TL, 1983, LENS RES, V1, P109
  • [8] BINARY-LIQUID PHASE-SEPARATION OF LENS PROTEIN SOLUTIONS
    BROIDE, ML
    BERLAND, CR
    PANDE, J
    OGUN, OO
    BENEDEK, GB
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (13) : 5660 - 5664
  • [9] PRELIMINARY X-RAY CRYSTALLOGRAPHIC STUDY OF BOVINE LENS PROTEIN, NU-CRYSTALLIN FRACTION-2
    CARLISLE, CH
    LINDLEY, PF
    MOSS, DS
    SLINGSBY, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1977, 110 (02) : 417 - 419
  • [10] CRYSTALLOGRAPHIC STUDY OF GAMMA-CRYSTALLINS FROM CALF LENS
    CHIRGADZE, YN
    NIKONOV, SV
    GARBER, MB
    RESHETNIKOVA, LS
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1977, 110 (03) : 619 - 624