THE STRUCTURE OF RAT ADP-RIBOSYLATION-FACTOR-I (ARF-1) COMPLEXED TO GDP DETERMINED FROM 2 DIFFERENT CRYSTAL FORMS

被引:99
作者
GREASLEY, SE
JHOTI, H
TEAHAN, C
SOLARI, R
FENSOME, A
THOMAS, GMH
COCKCROFT, S
BAX, B
机构
[1] GLAXO INC, RES & DEV, DEPT BIOMOLEC STRUCT, STEVENAGE SG1 2NY, HERTS, ENGLAND
[2] MED RES CTR, DEPT CELLULAR SCI, STEVENAGE SG1 2NY, HERTS, ENGLAND
[3] UCL, DEPT PHYSIOL, LONDON WC1G 6JJ, ENGLAND
[4] UNIV LONDON BIRKBECK COLL, DEPT CRYSTALLOG, LONDON WC1E 7HX, ENGLAND
来源
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 09期
基金
英国惠康基金;
关键词
D O I
10.1038/nsb0995-797
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ARFs are a family of 21,000 M(r) proteins with biological roles in constitutive secretion and activation of phospholipase D. The structure of ARF-1 complexed to GDP determined from two crystal forms reveals a topology that is similar to that of the protein p21 ras with two differences: an additional amino-terminal helix and an extra beta-strand. The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is not seen in p21 ras, due to a shift in the relative position of the DXXG motif between the two proteins. The occurrence of a dimer in one crystal form suggests that ARF-1 may dimerize during its biological function. The dimer interface involves a region of the ARF-1 molecule that is analogous to the effector domain in p21 ras and may mediate interactions with its effectors.
引用
收藏
页码:797 / 806
页数:10
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