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TitleStructural insights into the activity of enhancer-binding proteins.
Journal, issue, pagesScience, Vol. 307, Issue 5717, Page 1972-1975, Year 2005
Publish dateMar 25, 2005
AuthorsMathieu Rappas / Jorg Schumacher / Fabienne Beuron / Hajime Niwa / Patricia Bordes / Sivaramesh Wigneshweraraj / Catherine A Keetch / Carol V Robinson / Martin Buck / Xiaodong Zhang /
PubMed AbstractActivators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic ...Activators of bacterial sigma54-RNA polymerase holoenzyme are mechanochemical proteins that use adenosine triphosphate (ATP) hydrolysis to activate transcription. We have determined by cryogenic electron microscopy (cryo-EM) a 20 angstrom resolution structure of an activator, phage shock protein F [PspF(1-275)], which is bound to an ATP transition state analog in complex with its basal factor, sigma54. By fitting the crystal structure of PspF(1-275) at 1.75 angstroms into the EM map, we identified two loops involved in binding sigma54. Comparing enhancer-binding structures in different nucleotide states and mutational analysis led us to propose nucleotide-dependent conformational changes that free the loops for association with sigma54.
External linksScience / PubMed:15790859 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.7 - 20.0 Å
Structure data

EMDB-1109:
Structural insights into the activity of enhancer-binding proteins.
Method: EM (single particle) / Resolution: 20.0 Å

PDB-2bjv:
Crystal Structure of PspF(1-275) R168A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-2bjw:
PspF AAA domain
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli (E. coli)
KeywordsTRANSCRIPTION / AAA / TRANSCRIPTION ACTIVATION / GENE REGULATION / SIGMA54 ACTIVATOR / ENHANCER BINDING PROTEIN / PSPF / ATP-BINDING / DNA- BINDING / TRANSCRIPTION REGULATION

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