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Structure paper

TitleStructure of apo-CAP reveals that large conformational changes are necessary for DNA binding
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 106, Page 16604-16609, Year 2009
Publish dateJan 17, 2009 (structure data deposition date)
AuthorsSharma, H. / Yu, S. / Kong, J. / Wang, J. / Steitz, T.A.
External linksProc. Natl. Acad. Sci. USA / PubMed:19805344
MethodsX-ray diffraction
Resolution2.3 - 3.59 Å
Structure data

PDB-3fwe:
Crystal Structure of the Apo D138L CAP mutant
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3hif:
The crystal structure of apo wild type CAP at 3.6 A resolution.
Method: X-RAY DIFFRACTION / Resolution: 3.59 Å

Chemicals

ChemComp-PRO:
PROLINE

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli (E. coli)
KeywordsTRANSCRIPTION REGULATOR / helix-turn-helix / transcription / cAMP / allostery / Acetylation / Activator / cAMP-binding / DNA-binding / Nucleotide-binding / Transcription regulation / cAMP binding domain

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