2KB4

NMR structure of the unphosphorylated form of OdhI, OdhI.

Summary for 2KB4

• Entry DOI: 10.2210/pdb2kb4/pdb
• NMR Information: BMRB: 16039
• Descriptor: Oxoglutarate dehydrogenase inhibitor (1 entity in total)
• Functional Keywords: forkhead-associated domain, kinase substrate, gara, fha, phosphoprotein, dehydrogenase inhibitor
• Biological source: Corynebacterium glutamicum (Brevibacterium flavum)
• Total number of polymer chains: 1
• Total formula weight: 15417.02

Authors

Barthe, P.,Roumestand, C.,Canova, M.,Hurard, C.,Molle, V.,Cohen-Gonsaud, M. (deposition date: 2008-11-20, release date: 2009-05-05, Last modification date: 2024-05-08)

Primary citation

Barthe, P.,Roumestand, C.,Canova, M.J.,Kremer, L.,Hurard, C.,Molle, V.,Cohen-Gonsaud, M.
Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism.
Structure, 17:568-578, 2009

PubMed Abstract: 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.

PubMed: 19368890
DOI: 10.1016/j.str.2009.02.012

Experimental method

SOLUTION NMR