2WHS
Fluorescent Protein mKeima at pH 3.8
2WHS の概要
| エントリーDOI | 10.2210/pdb2whs/pdb |
| 関連するPDBエントリー | 2WHT 2WHU |
| 分子名称 | LARGE STOKES SHIFT FLUORESCENT PROTEIN, SULFATE ION (3 entities in total) |
| 機能のキーワード | fluorescent protein, stokes shift, mkeima |
| 由来する生物種 | Montipora sp. 20 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 109983.44 |
| 構造登録者 | Violot, S.,Carpentier, P.,Blanchoin, L.,Bourgeois, D. (登録日: 2009-05-06, 公開日: 2009-08-11, 最終更新日: 2024-11-13) |
| 主引用文献 | Violot, S.,Carpentier, P.,Blanchoin, L.,Bourgeois, D. Reverse Ph-Dependence of Chromophore Protonation Explains the Large Stokes Shift of the Red Fluorescent Protein Mkeima. J.Am.Chem.Soc., 131:10356-, 2009 Cited by PubMed Abstract: The recently developed red fluorescent protein Keima exhibits the largest Stokes shift (180 nm) observed to date. Combining X-ray crystallography with (in crystallo) UV-visible absorption, fluorescence, and Raman spectroscopy, we have investigated molecular determinants of this peculiar property. The results demonstrate a pH-dependent "reverse chromophore protonation" triggered by the key residue Asp157 and which couples to cis/trans isomerization of the chromophore. These data provided guidelines to rationally design a useful Keima variant. PubMed: 19722611DOI: 10.1021/JA903695N 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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