Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
Sharma H, Yu S, Kong J, Wang J, Steitz TA. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 16604-16609. PMID: 19805344, PMCID: PMC2745332, DOI: 10.1073/pnas.0908380106.Peer-Reviewed Original ResearchMeSH KeywordsApoproteinsBinding SitesCrystallography, X-RayCyclic AMPCyclic AMP Receptor ProteinDNAEscherichia coliEscherichia coli ProteinsLigandsModels, MolecularProtein ConformationConceptsColi catabolite gene activator proteinEscherichia coli catabolite gene activator proteinCatabolite gene activator proteinC-helixConformational changesGene activator proteinDNA binding domainsDNA recognition helixEarlier biochemical dataLarge conformational changesSpecific DNA sequencesBinding of cAMPRecognition helixActivator proteinDNA sequencesDNA bindingBinding domainsActive DNAWT structureInactive formInactive structureBiochemical dataDifferent conformationsBindingConformation