PRELIMINARY-X-RAY CRYSTALLOGRAPHIC ANALYSIS OF HOLOTOXIN FROM BORDETELLA-PERTUSSIS

被引:3
|
作者
RAGHAVAN, M [1 ]
GOTTO, JW [1 ]
SCOTT, JV [1 ]
SCHUTT, CE [1 ]
机构
[1] AMER CYANAMID CO,LEDERLE LABS,PEARL RIVER,NY 10965
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0022-2836(05)80204-9
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
Pertussis (whooping cough) is a serious infectious disease caused by the bacterium Bordetella pertussis. One of the major virulence factors is a protein known as pertussis toxin, which is composed of six subunits, with a total molecular weight of 106,000. Enzymatic transfer of ADP-ribose from NAD to a family of GTP-binding proteins is effected by the largest subunit (S1 or the A monomer), while binding of host cells and entry of S1 to the interior is a function of the other subunits (the B oligomer). The holotoxin crystallizes in the orthorhombic space group P212121, with unit cell dimensions a = 98·4 Å, b = 164·2 Å and c = 195·2 Å. The crystals are suitable for high-resolution X-ray diffraction analysis. © 1990 Academic Press Limited.
引用
收藏
页码:411 / 414
页数:4
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