1par

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File:1par.gif


1par, resolution 2.600Å

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DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE

OverviewOverview

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.

About this StructureAbout this Structure

1PAR is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.

ReferenceReference

DNA recognition by beta-sheets in the Arc repressor-operator crystal structure., Raumann BE, Rould MA, Pabo CO, Sauer RT, Nature. 1994 Feb 24;367(6465):754-7. PMID:8107872

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