3UG0
Crystal structure of a Trp-less green fluorescent protein translated by the simplified genetic code
Summary for 3UG0
| Entry DOI | 10.2210/pdb3ug0/pdb |
| Related | 3UFZ |
| Descriptor | Green fluorescent protein (2 entities in total) |
| Functional Keywords | green fluorescent protein, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 25626.88 |
| Authors | Kawahara-Kobayashi, A.,Araiso, Y.,Matsuda, T.,Yokoyama, S.,Kigawa, T.,Nureki, O.,Kiga, D. (deposition date: 2011-11-02, release date: 2012-10-17, Last modification date: 2024-11-20) |
| Primary citation | Kawahara-Kobayashi, A.,Masuda, A.,Araiso, Y.,Sakai, Y.,Kohda, A.,Uchiyama, M.,Asami, S.,Matsuda, T.,Ishitani, R.,Dohmae, N.,Yokoyama, S.,Kigawa, T.,Nureki, O.,Kiga, D. Simplification of the genetic code: restricted diversity of genetically encoded amino acids. Nucleic Acids Res., 40:10576-10584, 2012 Cited by PubMed Abstract: At earlier stages in the evolution of the universal genetic code, fewer than 20 amino acids were considered to be used. Although this notion is supported by a wide range of data, the actual existence and function of the genetic codes with a limited set of canonical amino acids have not been addressed experimentally, in contrast to the successful development of the expanded codes. Here, we constructed artificial genetic codes involving a reduced alphabet. In one of the codes, a tRNAAla variant with the Trp anticodon reassigns alanine to an unassigned UGG codon in the Escherichia coli S30 cell-free translation system lacking tryptophan. We confirmed that the efficiency and accuracy of protein synthesis by this Trp-lacking code were comparable to those by the universal genetic code, by an amino acid composition analysis, green fluorescent protein fluorescence measurements and the crystal structure determination. We also showed that another code, in which UGU/UGC codons are assigned to Ser, synthesizes an active enzyme. This method will provide not only new insights into primordial genetic codes, but also an essential protein engineering tool for the assessment of the early stages of protein evolution and for the improvement of pharmaceuticals. PubMed: 22909996DOI: 10.1093/nar/gks786 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.093 Å) |
Structure validation
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