1IXM
CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS
1IXM の概要
| エントリーDOI | 10.2210/pdb1ixm/pdb |
| 分子名称 | PROTEIN (SPORULATION RESPONSE REGULATORY PROTEIN) (1 entity in total) |
| 機能のキーワード | phosphotransferase, sporulation response regulator, two component system, regulatory protein, transferase |
| 由来する生物種 | Bacillus subtilis |
| 細胞内の位置 | Cytoplasm: P06535 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 45147.12 |
| 構造登録者 | |
| 主引用文献 | Varughese, K.I.,Madhusudan,Zhou, X.Z.,Whiteley, J.M.,Hoch, J.A. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol.Cell, 2:485-493, 1998 Cited by PubMed Abstract: A basis for understanding specificity of molecular recognition between phosphorelay proteins has been deduced from the 2.6 A structure of the Spo0B phosphotransferase of the phosphorelay regulating sporulation initiation. Spo0B consists of two domains: an N-terminal alpha-helical hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B dimerize by a parallel association of helical hairpins to form a novel four-helix bundle from which the active histidine protrudes. Docking studies show that both the monomers interact with a Spo0F molecule at the region surrounding the active site aspartate to position it for phosphotransfer. It is apparent that different surfaces of response regulators may be involved in recognition of the protein partners to which they are paired. PubMed: 9809070DOI: 10.1016/S1097-2765(00)80148-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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