4E7P
Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the presence of the phosphoryl analog beryllofluoride
4E7P の概要
エントリーDOI | 10.2210/pdb4e7p/pdb |
関連するPDBエントリー | 4E7O |
分子名称 | Response regulator, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (4 entities in total) |
機能のキーワード | dna binding, cytosol, transcription regulator |
由来する生物種 | Streptococcus pneumoniae |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 33977.57 |
構造登録者 | |
主引用文献 | Park, A.K.,Moon, J.H.,Lee, K.S.,Chi, Y.M. Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride. Biochem.Biophys.Res.Commun., 421:403-407, 2012 Cited by PubMed Abstract: Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded α/β fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814(R)) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814(R) was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814(R), resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814. PubMed: 22521891DOI: 10.1016/j.bbrc.2012.04.035 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.892 Å) |
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