Structural highlights
Function
[ODHI_CORGL] An essential component of the PknG signaling pathway. When unphosphorylated, it inhibits the activity of 2-oxoglutarate dehydrogenase. When phosphorylated it does not inhibit 2-oxoglutarate dehydrogenase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The OdhI 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 OdhI inhibits the OdhA protein, a key enzyme of the TCA cycle, whereas the phosphorylated form is inactive. OdhI 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.
Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism.,Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M Structure. 2009 Apr 15;17(4):568-78. PMID:19368890[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M. Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. Structure. 2009 Apr 15;17(4):568-78. PMID:19368890 doi:10.1016/j.str.2009.02.012
