2LC0
Rv0020c_Nter structure
2LC0 の概要
| エントリーDOI | 10.2210/pdb2lc0/pdb |
| 関連するPDBエントリー | 2LC1 |
| NMR情報 | BMRB: 17585 |
| 分子名称 | Putative uncharacterized protein TB39.8 (1 entity in total) |
| 機能のキーワード | fhaa, kinase substrate, protein binding |
| 由来する生物種 | Mycobacterium tuberculosis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14773.44 |
| 構造登録者 | Barthe, P.P.,Cohen-Gonsaud, M.M.,Roumestand, C. (登録日: 2011-04-11, 公開日: 2011-11-02, 最終更新日: 2024-05-29) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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