STRUCTURAL SIMILARITY OF A DEVELOPMENTALLY-REGULATED BACTERIAL SPORE COAT PROTEIN TO BETA-GAMMA-CRYSTALLINS OF THE VERTEBRATE EYE LENS

被引:39
作者
BAGBY, S
HARVEY, TS
EAGLE, SG
INOUYE, S
IKURA, M
机构
[1] UNIV TORONTO, ONTARIO CANC INST, DIV MOLEC & STRUCT BIOL, TORONTO M4X 1K9, ON, CANADA
[2] UNIV TORONTO, DEPT MED BIOPHYS, TORONTO M4X 1K9, ON, CANADA
[3] ROBERT WOOD JOHNSON MED SCH, DEPT BIOCHEM, PISCATAWAY, NJ 08854 USA
关键词
NUCLEAR MAGNETIC RESONANCE; MYXOCOCCUS XANTHUS; CALCIUM-BINDING PROTEIN; GREEK KEY; DIVERGENT EVOLUTION;
D O I
10.1073/pnas.91.10.4308
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
The solution structure of Ca2+-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy. Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twofold symmetry axis, overall resembling a triangular prism. Each domain consists of two topologically inequivalent ''Creek keys'': the second and fourth moths form standard Greek keys, whereas the first and third moths each contain a regular alpha-helix in addition to the usual four beta-strands. The structure of protein S is similar to those of the vertebrate eye lens beta gamma-crystallins, which are thought to be evolutionarily related to protein S. Both protein S and the beta gamma crystallins function by forming stable multimolecular assemblies. However, protein S possesses distinctive moth organization and domain packing, indicating a different mode of oligomerization and a divergent evolutionary pathway from the beta gamma-crystallins.
引用
收藏
页码:4308 / 4312
页数:5
相关论文
共 51 条
[1]   THE SOLUTION STRUCTURES OF ESCHERICHIA-COLI-TRP REPRESSOR AND TRP APOREPRESSOR AT AN INTERMEDIATE RESOLUTION [J].
ARROWSMITH, C ;
PACHTER, R ;
ALTMAN, R ;
JARDETZKY, O .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 202 (01) :53-66
[2]   UNUSUAL HELIX-CONTAINING GREEK KEYS IN DEVELOPMENT-SPECIFIC CA2+-BINDING PROTEIN-S - H-1, N-15, AND C-13 ASSIGNMENTS AND SECONDARY STRUCTURE DETERMINED WITH THE USE OF MULTIDIMENSIONAL DOUBLE AND TRIPLE-RESONANCE HETERONUCLEAR NMR-SPECTROSCOPY [J].
BAGBY, S ;
HARVEY, TS ;
KAY, LE ;
EAGLE, SG ;
INOUYE, S ;
IKURA, M .
BIOCHEMISTRY, 1994, 33 (09) :2409-2421
[3]   NMR-DERIVED 3-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN-S COMPLEXED WITH CALCIUM [J].
BAGBY, S ;
HARVEY, TS ;
EAGLE, SG ;
INOUYE, S ;
IKURA, M .
STRUCTURE, 1994, 2 (02) :107-122
[4]   HOMONUCLEAR BROADBAND-DECOUPLED ABSORPTION-SPECTRA, WITH LINEWIDTHS WHICH ARE INDEPENDENT OF THE TRANSVERSE RELAXATION RATE [J].
BAX, A ;
MEHLKOPF, AF ;
SMIDT, J .
JOURNAL OF MAGNETIC RESONANCE, 1979, 35 (01) :167-169
[5]   X-RAY-ANALYSIS OF BETA-B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS [J].
BAX, B ;
LAPATTO, R ;
NALINI, V ;
DRIESSEN, H ;
LINDLEY, PF ;
MAHADEVAN, D ;
BLUNDELL, TL ;
SLINGSBY, C .
NATURE, 1990, 347 (6295) :776-780
[6]   THE MOLECULAR-STRUCTURE AND STABILITY OF THE EYE LENS - X-RAY-ANALYSIS OF GAMMA-CRYSTALLIN-II [J].
BLUNDELL, T ;
LINDLEY, P ;
MILLER, L ;
MOSS, D ;
SLINGSBY, C ;
TICKLE, I ;
TURNELL, B ;
WISTOW, G .
NATURE, 1981, 289 (5800) :771-777
[7]  
BRUNGER AT, 1990, X PLOR MANUAL VERSIO
[8]   RIBBON MODELS OF MACROMOLECULES [J].
CARSON, M .
JOURNAL OF MOLECULAR GRAPHICS, 1987, 5 (02) :103-&
[9]  
CLORE GM, 1991, BIOCHEMISTRY-US, V30, P3215
[10]   AMINO-ACID SEQUENCE OF RABBIT SKELETAL-MUSCLE TROPONIN-C - GENE REPLICATION AND HOMOLOGY WITH CALCIUM-BINDING PROTEINS FROM CARP AND HAKE MUSCLE [J].
COLLINS, JH ;
POTTER, JD ;
HORN, MJ ;
WILSHIRE, G ;
JACKMAN, N .
FEBS LETTERS, 1973, 36 (03) :268-272