4H3L
mPlum-E16P
Summary for 4H3L
| Entry DOI | 10.2210/pdb4h3l/pdb |
| Related | 4H3M 4H3N |
| Descriptor | Fluorescent protein plum, SODIUM ION (3 entities in total) |
| Functional Keywords | fluorescent protein |
| Biological source | Discosoma sp. LW-2004 |
| Total number of polymer chains | 2 |
| Total formula weight | 53054.78 |
| Authors | Moore, M.M.,Chica, R.A. (deposition date: 2012-09-14, release date: 2012-10-31, Last modification date: 2023-12-06) |
| Primary citation | Moore, M.M.,Oteng-Pabi, S.K.,Pandelieva, A.T.,Mayo, S.L.,Chica, R.A. Recovery of Red Fluorescent Protein Chromophore Maturation Deficiency through Rational Design. Plos One, 7:e52463-e52463, 2012 Cited by PubMed Abstract: Red fluorescent proteins (RFPs) derived from organisms in the class Anthozoa have found widespread application as imaging tools in biological research. For most imaging experiments, RFPs that mature quickly to the red chromophore and produce little or no green chromophore are most useful. In this study, we used rational design to convert a yellow fluorescent mPlum mutant to a red-emitting RFP without reverting any of the mutations causing the maturation deficiency and without altering the red chromophore's covalent structure. We also created an optimized mPlum mutant (mPlum-E16P) that matures almost exclusively to the red chromophore. Analysis of the structure/function relationships in these proteins revealed two structural characteristics that are important for efficient red chromophore maturation in DsRed-derived RFPs. The first is the presence of a lysine residue at position 70 that is able to interact directly with the chromophore. The second is an absence of non-bonding interactions limiting the conformational flexibility at the peptide backbone that is oxidized during red chromophore formation. Satisfying or improving these structural features in other maturation-deficient RFPs may result in RFPs with faster and more complete maturation to the red chromophore. PubMed: 23285050DOI: 10.1371/journal.pone.0052463 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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