1DC9

PROPERTIES AND CRYSTAL STRUCTURE OF A BETA-BARREL FOLDING MUTANT, V60N INTESTINAL FATTY ACID BINDING PROTEIN (IFABP)

1DC9 の概要

• エントリーDOI: 10.2210/pdb1dc9/pdb
• 関連するPDBエントリー: 1ICM 1ICN 1IFB 1IFC 2IFB
• 分子名称: INTESTINAL FATTY ACID BINDING PROTEIN (2 entities in total)
• 機能のキーワード: fatty acid binding protein, intracellular lipid binding protein, mutant, beta- barrel, lipid binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P02693
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15029.99

構造登録者

Ropson, I.J.,Yowler, B.C.,Dalessio, P.M.,Banaszak, L.,Thompson, J. (登録日: 1999-11-04, 公開日: 2000-03-20, 最終更新日: 2024-02-07)

主引用文献

Ropson, I.J.,Yowler, B.C.,Dalessio, P.M.,Banaszak, L.,Thompson, J.
Properties and crystal structure of a beta-barrel folding mutant.
Biophys.J., 78:1551-1560, 2000

PubMed Abstract: A mutant of a beta-barrel protein, rat intestinal fatty acid binding protein, was predicted to be more stable than the wild-type protein due to a novel hydrogen bond. Equilibrium denaturation studies indicated the opposite: the V60N mutant protein was less stable. The folding transitions followed by CD and fluorescence were reversible and two-state for both mutant and wild-type protein. However, the rates of denaturation and renaturation of V60N were faster. During unfolding, the initial rate was associated with 75-80% of the fluorescence and all of the CD amplitude change. A subsequent rate accounted for the remaining fluorescence change for both proteins; thus the intermediate state lacked secondary structure. During folding, one rate was detected by both fluorescence and CD after an initial burst phase for both wild-type and mutant. An additional slower folding rate was detected by fluorescence for the mutant protein. The structure of the V60N mutant has been obtained and is nearly identical to prior crystal structures of IFABP. Analysis of mean differences in hydrogen bond and van der Waals interactions did not readily account for the stability loss due to the mutation. However, significant average differences of the solvent accessible surface and crystallographic displacement factors suggest entropic destabilization.

PubMed: 10692339

実験手法

X-RAY DIFFRACTION (2.1 Å)