3RWT
Crystal structure of circular permutated Red Fluorescent Protein mKate(cp 154-153)
Summary for 3RWT
| Entry DOI | 10.2210/pdb3rwt/pdb |
| Related | 3RWA |
| Descriptor | Fluorescent protein FP480,Fluorescent protein FP480, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | gfp-like fluorescent protein, mkate, circular permutated, red fluorescentprotein, fluorescent protein |
| Biological source | Entacmaea quadricolor (Bubble-tip anemone) More |
| Total number of polymer chains | 8 |
| Total formula weight | 212714.45 |
| Authors | Wang, Q.,Sondermann, H. (deposition date: 2011-05-09, release date: 2011-06-15, Last modification date: 2025-03-26) |
| Primary citation | Shui, B.,Wang, Q.,Lee, F.,Byrnes, L.J.,Chudakov, D.M.,Lukyanov, S.A.,Sondermann, H.,Kotlikoff, M.I. Circular permutation of red fluorescent proteins. Plos One, 6:e20505-e20505, 2011 Cited by PubMed Abstract: Circular permutation of fluorescent proteins provides a substrate for the design of molecular sensors. Here we describe a systematic exploration of permutation sites for mCherry and mKate using a tandem fusion template approach. Circular permutants retaining more than 60% (mCherry) and 90% (mKate) brightness of the parent molecules are reported, as well as a quantitative evaluation of the fluorescence from neighboring mutations. Truncations of circular permutants indicated essential N- and C-terminal segments and substantial flexibility in the use of these molecules. Structural evaluation of two cp-mKate variants indicated no major conformational changes from the previously reported wild-type structure, and cis conformation of the chromophores. Four cp-mKates were identified with over 80% of native fluorescence, providing important new building blocks for sensor and complementation experiments. PubMed: 21647365DOI: 10.1371/journal.pone.0020505 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
Download full validation report
