Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolution

A. Mondragón, S. Subbiah, Steven C. Almo, M. Drottar, S. C. Harrison

Research output: Contribution to journalArticle

126 Citations (Scopus)

Abstract

The crystal structure of the amino-terminal domain of phage 434 represser has been solved using molecular replacement methods and refined to an R-factor of 19.3% against data to 2.0 Å resolution. The protein comprises five short α-helices. Two of these form a helix-turn-helix motif, very similar to those found in related proteins. The protein is remarkably similar to the Cro protein from the same phage.

Original languageEnglish (US)
Pages (from-to)189-200
Number of pages12
JournalJournal of Molecular Biology
Volume205
Issue number1
DOIs
StatePublished - Jan 5 1989
Externally publishedYes

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Bacteriophages
R388
Proteins
Helix-Turn-Helix Motifs

ASJC Scopus subject areas

  • Virology

Cite this

Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolution. / Mondragón, A.; Subbiah, S.; Almo, Steven C.; Drottar, M.; Harrison, S. C.

In: Journal of Molecular Biology, Vol. 205, No. 1, 05.01.1989, p. 189-200.

Research output: Contribution to journalArticle

Mondragón, A. ; Subbiah, S. ; Almo, Steven C. ; Drottar, M. ; Harrison, S. C. / Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolution. In: Journal of Molecular Biology. 1989 ; Vol. 205, No. 1. pp. 189-200.
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