Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

Ekaterina V. Filippova; Maksymilian Chruszcz; Marcin Cymborowski; Jun Gu; Alexei Savchenko; Aled Edwards; Wladek Minor

doi:10.1007/s10969-011-9112-4

Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

Ekaterina V. Filippova, Maksymilian Chruszcz, Marcin Cymborowski, Jun Gu, Alexei Savchenko, Aled Edwards, Wladek Minor^*

^*Corresponding author for this work

Pharmacology

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

5 Scopus citations

Abstract

A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 Å resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function.

Original language	English (US)
Pages (from-to)	149-157
Number of pages	9
Journal	Journal of Structural and Functional Genomics
Volume	12
Issue number	3
DOIs	https://doi.org/10.1007/s10969-011-9112-4
State	Published - Sep 2011

Keywords

Helix-turn-helix DNA-binding motif
Structural genomics
TetR transcriptional regulator
X-ray crystal structure

ASJC Scopus subject areas

Genetics
Structural Biology
Biochemistry

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10.1007/s10969-011-9112-4

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title = "Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins",

abstract = "A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 {\AA} resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function.",

keywords = "Helix-turn-helix DNA-binding motif, Structural genomics, TetR transcriptional regulator, X-ray crystal structure",

author = "Filippova, {Ekaterina V.} and Maksymilian Chruszcz and Marcin Cymborowski and Jun Gu and Alexei Savchenko and Aled Edwards and Wladek Minor",

note = "Funding Information: Acknowledgments The results shown in this report are derived from work performed at Argonne National Laboratory, at the Structural Biology Center of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the US Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. The authors would like to thank Andrzej Joachimiak and members of the Structural Biology Center and the Midwest Center for Structural Genomics for help and discussions, and Matthew Zimmerman for critically reading the manuscript. The work described in the paper was supported by NIH PSI grants GM62414 and GM074942.",

year = "2011",

month = sep,

doi = "10.1007/s10969-011-9112-4",

language = "English (US)",

volume = "12",

pages = "149--157",

journal = "Journal of Structural and Functional Genomics",

issn = "1345-711X",

publisher = "Springer Netherlands",

number = "3",

}

Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins. / Filippova, Ekaterina V.; Chruszcz, Maksymilian; Cymborowski, Marcin et al.
In: Journal of Structural and Functional Genomics, Vol. 12, No. 3, 09.2011, p. 149-157.

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

TY - JOUR

T1 - Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

AU - Filippova, Ekaterina V.

AU - Chruszcz, Maksymilian

AU - Cymborowski, Marcin

AU - Gu, Jun

AU - Savchenko, Alexei

AU - Edwards, Aled

AU - Minor, Wladek

N1 - Funding Information: Acknowledgments The results shown in this report are derived from work performed at Argonne National Laboratory, at the Structural Biology Center of the Advanced Photon Source. Argonne is operated by University of Chicago Argonne, LLC, for the US Department of Energy, Office of Biological and Environmental Research under contract DE-AC02-06CH11357. The authors would like to thank Andrzej Joachimiak and members of the Structural Biology Center and the Midwest Center for Structural Genomics for help and discussions, and Matthew Zimmerman for critically reading the manuscript. The work described in the paper was supported by NIH PSI grants GM62414 and GM074942.

PY - 2011/9

Y1 - 2011/9

N2 - A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 Å resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function.

AB - A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 Å resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function.

KW - Helix-turn-helix DNA-binding motif

KW - Structural genomics

KW - TetR transcriptional regulator

KW - X-ray crystal structure

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ER -

Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

Abstract

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Crystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolor

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Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins

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Keywords

ASJC Scopus subject areas

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Crystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolor

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