期刊
STRUCTURE
卷 17, 期 4, 页码 568-578出版社
CELL PRESS
DOI: 10.1016/j.str.2009.02.012
关键词
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资金
- Agence National de la Recherche [JC07203251, ANR-06-MIME-027-01]
The Odhl protein is key regulator of the TCA cycle in Corynebacterium glutamicum. This highly conserved protein is found in GC rich Gram-positive bacteria (e.g., the pathogenic Mycobacterium tuberculosis). The unphosphorylated form of Odhl inhibits the OdhA protein, a key enzyme of the TCA cycle, whereas the phosphorylated form is inactive. Odhl is predicted to be mainly a single FHA domain, a module that mediates protein-protein interaction through binding of phosphothreonine peptides, with a disordered N-terminal extension substrate of the serine/threonine protein kinases. In this study, we solved the solution structure of the unphosphorylated and phosphorylated isoforms of the protein. We observed a major conformational change between the two forms characterized by the binding of the phosphorylated N-terminal part of the protein to its own FHA domain, consequently inhibiting it. This structural observation corresponds to a new autoinhibition mechanism described for a FHA domain protein.
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