1HYP

CRYSTAL STRUCTURE OF HYDROPHOBIC PROTEIN FROM SOYBEAN; A MEMBER OF A NEW CYSTINE-RICH FAMILY

1HYP の概要

• エントリーDOI: 10.2210/pdb1hyp/pdb
• 分子名称: HYDROPHOBIC PROTEIN FROM SOYBEAN (2 entities in total)
• 機能のキーワード: hydrophobic seed protein
• 由来する生物種: Glycine max (soybean)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8363.83

構造登録者

Lehmann, M.S. (登録日: 1993-02-05, 公開日: 1993-04-15, 最終更新日: 2024-10-30)

主引用文献

Baud, F.,Pebay-Peyroula, E.,Cohen-Addad, C.,Odani, S.,Lehmann, M.S.
Crystal structure of hydrophobic protein from soybean; a member of a new cysteine-rich family.
J.Mol.Biol., 231:877-887, 1993

PubMed Abstract: X-ray diffraction methods have been used to determine the structure of the 8.3 kDa hydrophobic protein from soybean and to refine the atomic co-ordinates to a crystallographic R-factor of 18.7% at 1.8 A resolution. The molecule is a four-helix bundle, which together with the connecting loops and a twisted beta-strand form a spiral. The surface contains 70% apolar atoms, and the crystal packing is dominated by hydrophobic interactions, producing a two-dimensional sheet of protein molecules. Most of the 59 water molecules located are involved in hydrophilic contacts and their structural organization does not seem to be affected by the high hydrophobicity of the molecule. From the protein fold it appears that three of the four disulphide bridges are important for keeping the amino and carboxyl-terminal segments in place in the native form, while the central part of the molecule is stabilized by many hydrophobic interactions. Although the protein function is not known, a number of possibilities can be excluded on experimental grounds and by comparison with other members of the family.

PubMed: 8515457
DOI: 10.1006/jmbi.1993.1334

実験手法

X-RAY DIFFRACTION (1.8 Å)