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Structure paper

TitleDomain-Domain Flexibility Leads to Allostery within the Cam Receptor Protein (Crp)
Journal, issue, pagesTo be Published
Publish dateApr 1, 2011 (structure data deposition date)
AuthorsKnapp, J. / White, M.A. / Lee, J.C.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.6 - 2.95 Å
Structure data

PDB-3rdi:
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3rou:
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3rpq:
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Method: X-RAY DIFFRACTION / Resolution: 2.61 Å

PDB-3ryp:
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3ryr:
Domain-domain flexibility leads to allostery within the camp receptor protein (CRP)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsTRANSCRIPTION REGULATOR / CAMP RECEPTOR PROTEIN (CRP) / ALLOSTERY / DNA BINDING CYCLIC AMP / CATABOLITE ACTIVATOR PROTEIN (CAP) / DNA BINDING PROTEIN

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