1G1I

CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4

1G1I の概要

• エントリーDOI: 10.2210/pdb1g1i/pdb
• 関連するPDBエントリー: 1G1J
• 分子名称: NON-STRUCTURAL GLYCOPROTEIN NSP4, CALCIUM ION (3 entities in total)
• 機能のキーワード: ns28, parallel coiled-coil, homo-tetramer, metal binding site, metal binding protein
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10848.59

構造登録者

Bowman, G.D.,Nodelman, I.M.,Schutt, C.E. (登録日: 2000-10-11, 公開日: 2001-01-10, 最終更新日: 2024-10-30)

主引用文献

Bowman, G.D.,Nodelman, I.M.,Levy, O.,Lin, S.L.,Tian, P.,Zamb, T.J.,Udem, S.A.,Venkataraghavan, B.,Schutt, C.E.
Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site.
J.Mol.Biol., 304:861-871, 2000

PubMed Abstract: During the maturation of rotaviral particles, non-structural protein 4 (NSP4) plays a critical role in the translocation of the immature capsid into the lumen of the endoplasmic reticulum. Full-length NSP4 and a 22 amino acid peptide (NSP4(114-135)) derived from this protein have been shown to induce diarrhea in young mice in an age-dependent manner, and may therefore be the agent responsible for rotavirally-induced symptoms. We have determined the crystal structure of the oligomerization domain of NSP4 which spans residues 95 to 137 (NSP4(95-137)). NSP4(95-137) self-associates into a parallel, tetrameric coiled-coil, with the hydrophobic core interrupted by three polar layers occupying a and d-heptad positions. Side-chains from two consecutive polar layers, consisting of four Gln123 and two of the four Glu120 residues, coordinate a divalent cation. Two independent structures built from MAD-phased data indicated the presence of a strontium and calcium ion bound at this site, respectively. This metal-binding site appears to play an important role in stabilizing the homo-tetramer, which has implications for the engagement of NSP4 as an enterotoxin.

PubMed: 11124032
DOI: 10.1006/jmbi.2000.4250

実験手法

X-RAY DIFFRACTION (2 Å)