2LC0
Rv0020c_Nter structure
Summary for 2LC0
| Entry DOI | 10.2210/pdb2lc0/pdb |
| Related | 2LC1 |
| NMR Information | BMRB: 17585 |
| Descriptor | Putative uncharacterized protein TB39.8 (1 entity in total) |
| Functional Keywords | fhaa, kinase substrate, protein binding |
| Biological source | Mycobacterium tuberculosis |
| Total number of polymer chains | 1 |
| Total formula weight | 14773.44 |
| Authors | Barthe, P.P.,Cohen-Gonsaud, M.M.,Roumestand, C. (deposition date: 2011-04-11, release date: 2011-11-02, Last modification date: 2024-05-29) |
| Primary citation | Roumestand, C.,Leiba, J.,Galophe, N.,Margeat, E.,Padilla, A.,Bessin, Y.,Barthe, P.,Molle, V.,Cohen-Gonsaud, M. Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase Structure, 19:1525-1534, 2011 Cited by PubMed Abstract: The protein Rv0020c from Mycobacterium tuberculosis, also called FhaA, is one of the major substrates of the essential Ser/Thr protein kinase (STPK) PknB. The protein is composed of three domains and is phosphorylated on a unique site in its N terminus. We solved the solution structure of both N- and C-terminal domains and demonstrated that the approximately 300 amino acids of the intermediate domain are not folded. We present evidence that the FHA, a phosphospecific binding domain, of Rv0020c does not interact with the phosphorylated catalytic domains of PknB, but with the phosphorylated juxtamembrane domain that links the catalytic domain to the mycobacterial membrane. We also demonstrated that the degree and the pattern of phosphorylation of this juxtamembrane domain modulates the affinity of the substrate (Rv0020c) toward its kinase (PknB). PubMed: 22000520DOI: 10.1016/j.str.2011.07.011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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