5B61

Extra-superfolder GFP

Summary for 5B61

Entry DOI	10.2210/pdb5b61/pdb
Descriptor	Green fluorescent protein (1 entity in total)
Functional Keywords	gfp, random mutagenesis, folding robustness, fluorescent protein
Biological source	Aequorea victoria (Jellyfish)
Total number of polymer chains	6
Total formula weight	160855.97
Authors	Park, H.H.,Jang, T.-H.,Choi, J.Y. (deposition date: 2016-05-24, release date: 2017-06-14, Last modification date: 2024-03-20)
Primary citation	Choi, J.Y.,Jang, T.-H.,Park, H.H. The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP. FEBS Lett., 591:442-447, 2017 Cited by PubMed Abstract: Stability of green fluorescent protein (GFP) is sometimes important for a proper practical application of this protein. Random mutagenesis and targeted mutagenesis have been used to create better-folded variants of GFP, including recently reported extra-superfolder GFP. Our aim was to determine the crystal structure of extra-superfolder GFP, which is more robustly folded and stable than GFP and superfolder GFP. The structural and structure-based mutagenesis analyses revealed that some of the mutations that created extra-superfolder GFP (F46L, E126K, N149K, and S208L) contribute to folding robustness by stabilizing extra-superfolder GFP with various noncovalent bonds. PubMed: 27990640 DOI: 10.1002/1873-3468.12534 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3.115 Å)

Structure validation