title: The mechanism of folding robustness revealed by the crystal structure of extra-superfolder GFP.
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.
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, South Korea.
authors.forename: Jae Young
authors.initials: JY
authors.lastname: Choi
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, South Korea.
authors.forename: Tae-Ho
authors.initials: TH
authors.lastname: Jang
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, South Korea.
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D055550:Protein Stability; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein; D013696:Temperature
chemical_list: D049452:Green Fluorescent Proteins
keywords: 
  GFP
  ; crystal structure; mutations; protein folding; superfolder GFP