X-RAY CRYSTALLOGRAPHY SHOWS THAT TRANSLATIONAL INITIATION-FACTOR IF3 CONSISTS OF 2 COMPACT ALPHA/BETA DOMAINS LINKED BY AN ALPHA-HELIX

被引：132

作者：

BIOU, V ^{[1
]}

SHU, F ^{[1
]}

RAMAKRISHNAN, V ^{[1
]}

机构：

[1] BROOKHAVEN NATL LAB,DEPT BIOL,UPTON,NY 11973

来源：

EMBO JOURNAL | 1995年 / 14卷 / 16期

关键词：

ANOMALOUS SCATTERING; MULTIWAVELENGTH ANOMALOUS DISPERSION; RIBOSOME; SELENOMETHIONINE; TRANSLATION;

D O I：

10.1002/j.1460-2075.1995.tb00077.x

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 structures of the two domains of translational initiation factor IF3 from Bacillus stearothermophilus have been solved by X-ray crystallography using single wavelength anomalous scattering and multiwavelength anomalous diffraction, Each of the two domains has an alpha/beta topology, with an exposed beta-sheet that is reminiscent of several ribosomal and other RNA binding proteins, An alpha-helix that protrudes out from the body of the N-terminal domain towards the C-terminal domain suggests that IF3 consists of two RNA binding domains connected by an alpha-helix and that it may bridge two regions of the ribosome. This represents the first high resolution structural information on a translational initiation factor.

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页码：4056 / 4064

页数：9

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