1XWO

crystal structrue of goose delta crystallin

1XWO の概要

• エントリーDOI: 10.2210/pdb1xwo/pdb
• 分子名称: Delta crystallin (2 entities in total)
• 機能のキーワード: alpha helix bundle, double dimer, lyase
• 由来する生物種: Anser anser anser (western graylag goose)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 205203.45

構造登録者

Lee, H.J.,Lai, Y.H.,Wu, S.Y.,Chang, G.G. (登録日: 2004-11-02, 公開日: 2005-10-18, 最終更新日: 2024-03-13)

主引用文献

Lee, H.J.,Lai, Y.H.,Wu, S.Y.,Chen, Y.H.
The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin
Biochem.J., 392:545-554, 2005

PubMed Abstract: Delta-crystallin is a soluble structural protein in avian eye lenses that confers special refractive properties. In the presence of GdmCl (guanidinium chloride), tetrameric delta-crystallin undergoes dissociation via a dimeric state to a monomeric molten globule intermediate state. The latter are denatured at higher GdmCl concentrations in a multi-state manner. In the present study, the X-ray structure of goose delta-crystallin was determined to 2.8 A (1 A=0.1 nm). In this structure the first 25 N-terminal residues interact with a hydrophobic cavity in a neighbouring molecule, stabilizing the quaternary structure of this protein. When these 25 residues were deleted this did not produce any gross structural changes, as judged by CD analysis, but slightly altered tryptophan fluorescence and ANS (8-anilino-1-naphthalenesulphonic acid) spectra. The dimeric form was significantly identified as judged by sedimentation velocity and nondenaturing gradient gel electrophoresis. This mutant had increased sensitivity to temperature denaturation and GdmCl concentrations of 0.3-1.0 M. This protein was destabilized about 3.3 kcal/mol (1 kcal=4.184 kJ) due to N-terminal truncation. After incubation at 37 degrees C N-terminal truncated proteins were prone to aggregation, suggesting the presence of the unstable dimeric conformation. An important role for the N-terminus in dimer assembly of goose delta-crystallin is proposed.

PubMed: 16101585
DOI: 10.1042/BJ20050860

実験手法

X-RAY DIFFRACTION (2.8 Å)