X-ray crystal structure of TTHB099, a CRP/FNR superfamily transcriptional regulator from thermus thermophilus HB8, reveals a DNA-binding protein with no required allosteric effector molecule-Reference-Cited by-同舟云学术

X-ray crystal structure of TTHB099, a CRP/FNR superfamily transcriptional regulator from thermus thermophilus HB8, reveals a DNA-binding protein with no required allosteric effector molecule

Published:2012-03-01 Issue:5 Volume:80 Page:1490-1494
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Agari Yoshihiro,Kuramitsu Seiki,Shinkai Akeo

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.24049/fullpdf

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2. Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs;Körner;FEMS Microbiol Rev,2003

3. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding;Sharma;Proc Natl Acad Sci USA,2009

4. Structural basis for cAMP-mediated allosteric control of the catabolite activator protein;Popovych;Proc Natl Acad Sci USA,2009

5. Description of Thermus thermophilus (Yoshida and Oshima) com. nov., a non-sporulating thermophilic bacterium from a Japanese thermal spa;Oshima;Int J Syst Bacteriol,1974

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