HealthGate Document

Title

DNA recognition by beta-sheets in the Arc repressor-operator crystal structure.

Author

Raumann BE; Rould MA; Pabo CO; Sauer RT

Address

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Source

Nature, 1994 Feb 24, 367:6465, 754-7

Abstract

Transcription of the ant gene during lytic growth of bacteriophage P22 (ref. 1) is regulated by the cooperative binding of two Arc repressor dimers to a 21-base-pair operator site. Here we report the co-crystal structure of this Arc tetramer-operator complex at 2.6 A resolution. As expected from genetic and structural studies and from the co-crystal structure of the homologous Escherichia coli MetJ repressor, each Arc dimer uses an antiparallel beta-sheet to recognize bases in the major groove. However, the Arc and MetJ complexes differ in several important ways: the beta-sheet-DNA interactions of Arc are far less symmetrical; DNA binding by Arc is accompanied by important conformational changes in the beta-sheet; and Arc uses a different part of its protein surface for dimer-dimer interactions.

Language of Publication

English

Unique Identifier

94150708

MeSH Heading (Major)

DNA|*ME; Repressor Proteins|*CH; Viral Proteins|*CH

MeSH Heading

Base Sequence; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; Operator Regions (Genetics); Protein Structure, Secondary; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0028-0836

Country of Publication

ENGLAND

CAS Registry/EC Number

0 (phage repressor proteins); 0 (Repressor Proteins); 0 (Viral Proteins); 9007-49-2 (DNA)

Return to the HealthGate Home Page.