Structural Understanding of the Allosteric Conformational Change of Cyclic AMP Receptor Protein by Cyclic AMP Binding
| Autor: | Bong-Jin Lee, Y. Kyogoku, Mi-Kyung Yoon, T. Yamazaki, Hyung-Sik Won, Sang-Ho Park, Tae-Woo Lee |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Conformational change
Binding Sites Cyclic AMP Receptor Protein Nitrogen Isotopes Protein Conformation Chemistry Stereochemistry Protein subunit Molecular Sequence Data Allosteric regulation Amides Biochemistry Protein Structure Secondary Structure-Activity Relationship Protein structure Allosteric Regulation Cyclic AMP Amino Acid Sequence Protons Binding site Apoproteins Protein kinase A Nuclear Magnetic Resonance Biomolecular Protein secondary structure |
| Zdroj: | Biochemistry. 39:13953-13962 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi000012x |
| Popis: | Cyclic AMP receptor protein (CRP) plays a key role in the regulation of more than 150 genes. CRP is allosterically activated by cyclic AMP and binds to specific DNA sites. A structural understanding of this allosteric conformational change, which is essential for its function, is still lacking because the structure of apo-CRP has not been solved. Therefore, we performed various NMR experiments to obtain apo-CRP structural data. The secondary structure of apo-CRP was determined by analyses of the NOE connectivities, the amide proton exchange rates, and the (1)H-(15)N steady-state NOE values. A combination of the CSI-method and TALOS prediction was also used to supplement the determination of the secondary structure of apo-CRP. This secondary structure of apo-CRP was compared with the known structure of cyclic AMP-bound CRP. The results suggest that the allosteric conformational change of CRP caused by cyclic AMP binding involves subunit realignment and domain rearrangement, resulting in the exposure of helix F onto the surface of the protein. Additionally, the results of the one-dimensional [(13)C]carbonyl NMR experiments show that the conformational change of CRP caused by the binding of cyclic GMP, an analogue of cyclic AMP, is different from that caused by cyclic AMP binding. |
| Databáze: | OpenAIRE |
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