DNA RECOGNITION BY GAL4 - STRUCTURE OF A PROTEIN DNA COMPLEX

被引：573

作者：

MARMORSTEIN, R ^{[1
]}

CAREY, M ^{[1
]}

PTASHNE, M ^{[1
]}

HARRISON, SC ^{[1
]}

机构：

[1] HOWARD HUGHES MED INST, CAMBRIDGE, MA 02138 USA

来源：

NATURE | 1992年 / 356卷 / 6368期

关键词：

D O I：

10.1038/356408a0

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：

A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 angstrom resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn2+-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

引用

页码：408 / 414

页数：7

共 63 条

[41] NUCLEOTIDE-SEQUENCE OF THE ARGRII REGULATORY GENE AND AMINO-ACID-SEQUENCE HOMOLOGIES BETWEEN ARGRII PPRI AND GAL4 REGULATORY PROTEINS [J].