1VPS

POLYOMAVIRUS VP1 PENTAMER COMPLEXED WITH A DISIALYLATED HEXASACCHARIDE

1VPS の概要

• エントリーDOI: 10.2210/pdb1vps/pdb
• 分子名称: POLYOMAVIRUS VP1 PENTAMER, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-[N-acetyl-alpha-neuraminic acid-(2-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: virus coat protein, oligosaccharide binding, virus assembly, sialic acid, viral protein
• 由来する生物種: Murine polyomavirus
• 細胞内の位置: Virion: P49302
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 165265.36

構造登録者

Stehle, T.,Harrison, S.C. (登録日: 1997-03-07, 公開日: 1997-05-15, 最終更新日: 2024-05-22)

主引用文献

Stehle, T.,Harrison, S.C.
High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding.
Embo J., 16:5139-5148, 1997

PubMed Abstract: The crystal structure of a recombinant polyomavirus VP1 pentamer (residues 32-320) in complex with a branched disialylated hexasaccharide receptor fragment has been determined at 1.9 A resolution. The result extends our understanding of oligosaccharide receptor recognition. It also suggests a mechanism for enhancing the fidelity of virus assembly. We have previously described the structure of the complete polyomavirus particle complexed with this receptor fragment at 3.65 A. The model presented here offers a much more refined view of the interactions that determine carbohydrate recognition and allows us to assign additional specific contacts, in particular those involving the (alpha2,6)-linked, branching sialic acid. The structure of the unliganded VP1 pentamer, determined independently, shows that the oligosaccharide fits into a preformed groove and induces no measurable structural rearrangements. A comparison with assembled VP1 in the virus capsid reveals a rearrangement of residues 32-45 at the base of the pentamer. This segment may help prevent the formation of incorrectly assembled particles by reducing the likelihood that the C-terminal arm will fold back into its pentamer of origin.

PubMed: 9305654
DOI: 10.1093/emboj/16.16.5139

実験手法

X-RAY DIFFRACTION (1.9 Å)