Three-dimensional structure of a pre-catalytic human spliceosomal complex B

被引:61
作者
Boehringer, D [1 ]
Makarov, EM [1 ]
Sander, B [1 ]
Makarova, OV [1 ]
Kastner, B [1 ]
Lührmann, R [1 ]
Stark, H [1 ]
机构
[1] Max Planck Inst Biophys Chem, Dept Cellular Biochem, D-37077 Gottingen, Germany
关键词
D O I
10.1038/nsmb761
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
Major structural changes occur in the spliceosome during its transition from the fully assembled complex B to the catalytically activated spliceosome. To understand the rearrangement, it is necessary to know the detailed three-dimensional structures of these complexes. Here, we have immunoaffinity-purified human spliceosomes (designated BDeltaU1) at a stage after U4/U6.U5 tri-snRNP integration but before activation, and have determined the three-dimensional structure of BDeltaU1 by single-particle electron cryomicroscopy at a resolution of similar to40 Angstrom. The overall size of the complex is about 370 x 270 x 170 Angstrom. The three-dimensional structure features a roughly triangular body linked to a head domain in variable orientations. The body is very similar in size and shape to the isolated U4/U6.U5 tri-snRNP. This provides initial insight into the structural organization of complex B.
引用
收藏
页码:463 / 468
页数:6
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