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Structure paper

TitleStructural Insights into the Mechanism of the Allosteric Transitions of Mycobacterium tuberculosis cAMP Receptor Protein.
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 36581-36591, Year 2009
Publish dateJul 3, 2009 (structure data deposition date)
AuthorsReddy, M.C. / Palaninathan, S.K. / Bruning, J.B. / Thurman, C. / Smith, D. / Sacchettini, J.C.
External linksJ. Biol. Chem. / PubMed:19740754
MethodsX-ray diffraction
Resolution2.2 - 2.29 Å
Structure data

PDB-3i54:
Crystal structure of MtbCRP in complex with cAMP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3i59:
Crystal structure of MtbCRP in complex with N6-cAMP
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

Chemicals

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

ChemComp-HOH:
WATER

ChemComp-N6R:
(2R)-N6-(1-Methyl-2-phenylethyl)adenosine-3',5'-cyclic monophosphate

ChemComp-CL:
Unknown entry

ChemComp-N6S:
(2S)-N6-(1-Methyl-2-phenylethyl)adenosine-3',5'-cyclic monophosphate

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsDNA BINDING PROTEIN / Mycobacterium tuberculosis / cAMP Receptor Protein / allosteric mechanism / DNA binding / inhibition / Structural Genomics / TB Structural Genomics Consortium / TBSGC / DNA-binding / Transcription / Transcription regulation / CRP / N6-cAMP

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