The role of loops 3 and 4 in the interdomains and intersubunits communication of E. coli cAMP receptor protein.
Cyclic AMP serves as an intracellular messenger in cells and regulates a variety of biological functions by transmitting information through proteins. These proteins of different functions all consist of a cAMP-binding motif, and the structure of this motif is highly conserved with an exception of the loop 3 and 4. In current study, cAMP receptor protein was employed as a model system to investigate the function of the two loops. The results indicated that the loop 3 involves in the intersubunits communication of CRP, whereas the loop 4 involves in cAMP binding and interdomains communication.
Shen
Xianrong
X
Department of Chemistry, Fudan University, Shanghai 200433, China.
Tao
Wenbing
W
Kong
Jilie
J
Yu
Shaoning
S
D020816:Amino Acid Motifs; D016880:Anisotropy; D000242:Cyclic AMP / Q000737:chemistry; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry*; D004247:DNA / Q000737:chemistry; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008856:Microscopy, Fluorescence / Q000379:methods; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013816:Thermodynamics
D002373:Cyclic AMP Receptor Protein; D008024:Ligands; D004247:DNA; D000242:Cyclic AMP