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

A. Mondragón; S. Subbiah; S. C. Almo; M. Drottar; S. C. Harrison

doi:10.1016/0022-2836(89)90375-6

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

A. Mondragón^*, S. Subbiah, S. C. Almo, M. Drottar, S. C. Harrison

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

136 Scopus citations

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 language	English (US)
Pages (from-to)	189-200
Number of pages	12
Journal	Journal of Molecular Biology
Volume	205
Issue number	1
DOIs	https://doi.org/10.1016/0022-2836(89)90375-6
State	Published - Jan 5 1989

Funding

We thank J. Anderson, ,J. Kuriyan and C. Thorpe for their help during the various stages of this project, and M. Blum for his assistance with the area detector. We thank A. Aggarwal for many helpful discussions, and M. Ptashnr for support. encouragement and collaboration. A. M. is a Damon Runyon-Walter Winchell Cancer Fund Fellow (DRG-878). This work was supported by NIH grant GM29109 (to S.C.H. and M. Ptashne) and X;F;F grant CHE8509574 (to S.C.H., M. Karplus and D. Wiley).

ASJC Scopus subject areas

Molecular Biology
Biophysics
Structural Biology

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10.1016/0022-2836(89)90375-6

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title = "Structure of the amino-terminal domain of phage 434 represser at 2.0 {\AA} resolution",

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 {\AA} 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.",

author = "A. Mondrag{\'o}n and S. Subbiah and Almo, {S. C.} and M. Drottar and Harrison, {S. C.}",

note = "Funding Information: We thank J. Anderson, ,J. Kuriyan and C. Thorpe for their help during the various stages of this project, and M. Blum for his assistance with the area detector. We thank A. Aggarwal for many helpful discussions, and M. Ptashnr for support. encouragement and collaboration. A. M. is a Damon Runyon-Walter Winchell Cancer Fund Fellow (DRG-878). This work was supported by NIH grant GM29109 (to S.C.H. and M. Ptashne) and X;F;F grant CHE8509574 (to S.C.H., M. Karplus and D. Wiley).",

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doi = "10.1016/0022-2836(89)90375-6",

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T1 - Structure of the amino-terminal domain of phage 434 represser at 2.0 Å resolution

AU - Mondragón, A.

AU - Subbiah, S.

AU - Almo, S. C.

AU - Drottar, M.

AU - Harrison, S. C.

N1 - Funding Information: We thank J. Anderson, ,J. Kuriyan and C. Thorpe for their help during the various stages of this project, and M. Blum for his assistance with the area detector. We thank A. Aggarwal for many helpful discussions, and M. Ptashnr for support. encouragement and collaboration. A. M. is a Damon Runyon-Walter Winchell Cancer Fund Fellow (DRG-878). This work was supported by NIH grant GM29109 (to S.C.H. and M. Ptashne) and X;F;F grant CHE8509574 (to S.C.H., M. Karplus and D. Wiley).

PY - 1989/1/5

Y1 - 1989/1/5

N2 - 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.

AB - 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.

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

Abstract

Funding

ASJC Scopus subject areas

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