2DUE
crystal structure of a green fluorescent protein variant S65T/H148D at pH 10
Summary for 2DUE
| Entry DOI | 10.2210/pdb2due/pdb |
| Related | 2DUF 2DUG 2DUH 2DUI |
| Descriptor | Green fluorescent protein (2 entities in total) |
| Functional Keywords | excited state proton transfer, very short hydrogen bond, green fluorescent protein, luminescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 26923.33 |
| Authors | Shu, X.,Remington, S.J. (deposition date: 2006-07-23, release date: 2007-07-10, Last modification date: 2024-10-30) |
| Primary citation | Shu, X.,Kallio, K.,Shi, X.,Abbyad, P.,Kanchanawong, P.,Childs, W.,Boxer, S.G.,Remington, S.J. Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies. Biochemistry, 46:12005-12013, 2007 Cited by PubMed Abstract: Wild type green fluorescent protein (wt-GFP) and the variant S65T/H148D each exhibit two absorption bands, A and B, which are associated with the protonated and deprotonated chromophores, respectively. Excitation of either band leads to green emission. In wt-GFP, excitation of band A ( approximately 395 nm) leads to green emission with a rise time of 10-15 ps, due to excited-state proton transfer (ESPT) from the chromophore hydroxyl group to an acceptor. This process produces an anionic excited-state intermediate I* that subsequently emits a green photon. In the variant S65T/H148D, the A band absorbance maximum is red-shifted to approximately 415 nm, and as detailed in the accompanying papers, when the A band is excited, green fluorescence appears with a rise time shorter than the instrument time resolution ( approximately 170 fs). On the basis of the steady-state spectroscopy and high-resolution crystal structures of several variants described herein, it is proposed that in S65T/H148D, the red shift of absorption band A and the ultrafast appearance of green fluorescence upon excitation of band A are due to a very short ( DOI: 10.1021/bi7009037 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.24 Å) |
Structure validation
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