4NQW
Structure of Mycobacterium tuberculosis extracytoplasmic function sigma factor SigK in complex with the cytosolic domain of its cognate anti-sigma factor RskA
「3VDO」から置き換えられました4NQW の概要
エントリーDOI | 10.2210/pdb4nqw/pdb |
分子名称 | ECF RNA polymerase sigma factor SigK, Anti-sigma-K factor RskA, CADMIUM ION, ... (4 entities in total) |
機能のキーワード | sigma factor, transcription initiation, dna binding, promoter dna binding and transcription initiation, anti-sigma factor, dna binding protein-protein binding complex, dna binding protein/protein binding |
由来する生物種 | Mycobacterium tuberculosis 詳細 |
細胞内の位置 | Cell membrane; Single-pass membrane protein (Potential): O53729 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 32651.35 |
構造登録者 | |
主引用文献 | Shukla, J.,Gupta, R.,Thakur, K.G.,Gokhale, R.,Gopal, B. Structural basis for the redox sensitivity of the Mycobacterium tuberculosis SigK-RskA sigma-anti-sigma complex Acta Crystallogr.,Sect.D, 70:1026-1036, 2014 Cited by PubMed Abstract: The host-pathogen interactions in Mycobacterium tuberculosis infection are significantly influenced by redox stimuli and alterations in the levels of secreted antigens. The extracytoplasmic function (ECF) σ factor σ(K) governs the transcription of the serodominant antigens MPT70 and MPT83. The cellular levels of σ(K) are regulated by the membrane-associated anti-σ(K) (RskA) that localizes σ(K) in an inactive complex. The crystal structure of M. tuberculosis σ(K) in complex with the cytosolic domain of RskA (RskAcyto) revealed a disulfide bridge in the -35 promoter-interaction region of σ(K). Biochemical experiments reveal that the redox potential of the disulfide-forming cysteines in σ(K) is consistent with its role as a sensor. The disulfide bond in σ(K) influences the stability of the σ(K)-RskAcyto complex but does not interfere with σ(K)-promoter DNA interactions. It is noted that these disulfide-forming cysteines are conserved across homologues, suggesting that this could be a general mechanism for redox-sensitive transcription regulation. PubMed: 24699647DOI: 10.1107/S1399004714000121 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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