Structural overview on the allosteric activation of cyclic AMP receptor protein.
Cyclic AMP receptor protein (CRP) is a prokaryotic global transcription regulator that controls the expression of nearly 200 genes. The protein, allosterically activated by cAMP binding, binds to DNA and interacts with RNA polymerase. Current understanding on the allosteric process of the Escherichia coli CRP activation can be summarized into a rigid-body movement that involves subunit realignment and domain rearrangement. The main consequence of that overall transition is protrusion and adjustment of F-helices that recognize specific DNA sites. Although physicochemical and structural studies during the past decades have contributed to a comprehensive understanding of the CRP allostery, a paucity of structural information about the cAMP-free form (apo-CRP) has precluded a definite elucidation of the allosterism. In this respect, recent achievements of structures on other CRP-family proteins provide useful information to fill in the details of the allosteric transition of CRP. Thus, in this paper, accomplishments of CRP-family structures are summarized and inspected comparatively with new findings. This review not only provides a structural overview on the allosteric conformational change of CRP but also suggests a thoughtful discussion about unsolved issues or conflicting arguments. Solving those issues and the apo-CRP structure would enable us to finally define the CRP allostery.
Department of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea.
Hyung-Sik
HS
Won
Yoo-Sup
YS
Lee
Sung-Hee
SH
Lee
Bong-Jin
BJ
Lee
D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D002373:Cyclic AMP Receptor Protein / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment
D001426:Bacterial Proteins; D002373:Cyclic AMP Receptor Protein