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Structure paper

TitleAllostery and intrinsic disorder mediate transcription regulation by conditional cooperativity.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 142, Page 101-111, Year 2010
Publish dateJun 10, 2009 (structure data deposition date)
AuthorsGarcia-Pino, A. / Balasubramanian, S. / Wyns, L. / Gazit, E. / De Greve, H. / Magnuson, R.D. / Charlier, D. / van Nuland, N.A. / Loris, R.
External linksCell(Cambridge,Mass. ) / PubMed:20603017
MethodsX-ray diffraction
Resolution2.2 - 2.4 Å
Structure data

PDB-3hry:
Crystal structure of PHD in a trigonal space group and partially disordered
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-3hs2:
Crystal structure of PHD truncated to residue 57 in an orthorhombic space group
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3k33:
Crystal structure of the Phd-Doc complex
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-ACT:
ACETATE ION

Source
  • escherichia coli (E. coli)
  • enterobacteria phage p1 (virus)
  • unidentified (others)
KeywordsANTITOXIN / Phd / Prevent Host Death / intrinsic disorder / DOC / toxin-antitoxin / TOXIN/ANTITOXIN / Fic / toxin / allostery / transcription regulation / ribosome inhibitor / TOXIN-ANTITOXIN COMPLEX

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