PMID:10997904
| Citation |
Zapf, J, Sen, U, Madhusudan, , Hoch, JA and Varughese, KI (2000) A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction. Structure 8:851-62 |
|---|---|
| Abstract |
Spo0F and Spo0B specifically exchange a phosphoryl group in a central step of the phosphorelay signal transduction system that controls sporulation in Bacilli. Spo0F belongs to the superfamily of response regulator proteins and is one of 34 such proteins in Bacillus subtilis. Spo0B is structurally similar to the phosphohistidine domain of histidine kinases, such as EnvZ, and exchanges a phosphoryl group between His30 and Asp54 on Spo0F. Information at the molecular level on the interaction between response regulators and phosphohistidine domains is necessary to develop a rationale for how phospho-signaling fidelity is maintained in two-component systems. |
| Links | |
| Keywords |
Bacillus subtilis/chemistry; Bacillus subtilis/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein Conformation; Signal Transduction |
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