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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U2 - 10.1007/s10969-011-9112-4
DO - 10.1007/s10969-011-9112-4
M3 - Article
C2 - 21625866
AN - SCOPUS:80054873723
VL - 12
SP - 149
EP - 157
JO - Journal of Structural and Functional Genomics
JF - Journal of Structural and Functional Genomics
SN - 1345-711X
IS - 3
ER -