1NSB

THE 2.2 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF INFLUENZA B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC ACID

1NSB の概要

• エントリーDOI: 10.2210/pdb1nsb/pdb
• 分子名称: NEURAMINIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase(o-glycosyl)
• 由来する生物種: Influenza B virus (STRAIN B/BEIJING/1/87)
• 細胞内の位置: Virion membrane : P27907
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87421.16

構造登録者

Burmeister, W.P.,Ruigrok, R.W.H.,Cusack, S. (登録日: 1991-08-08, 公開日: 1993-10-31, 最終更新日: 2024-11-20)

主引用文献

Burmeister, W.P.,Ruigrok, R.W.,Cusack, S.
The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid.
EMBO J., 11:49-56, 1992

PubMed Abstract: Influenza virus neuraminidase catalyses the cleavage of terminal sialic acid, the viral receptor, from carbohydrate chains on glycoproteins and glycolipids. We present the crystal structure of the enzymatically active head of influenza B virus neuraminidase from the strain B/Beijing/1/87. The native structure has been refined to a crystallographic R-factor of 14.8% at 2.2 A resolution and its complex with sialic acid refined at 2.8 A resolution. The overall fold of the molecule is very similar to the already known structure of neuraminidase from influenza A virus, with which there is amino acid sequence homology of approximately 30%. Two calcium binding sites have been identified. One of them, previously undescribed, is located between the active site and a large surface antigenic loop. The calcium ion is octahedrally co-ordinated by five oxygen atoms from the protein and one water molecule. Sequence comparisons suggest that this calcium site should occur in all influenza A and B virus neuraminidases. Soaking of sialic acid into the crystals has enabled the mode of binding of the reaction product in the putative active site pocket to be revealed. All the large side groups of the sialic acid are equatorial and are specifically recognized by nine fully conserved active site residues. These in turn are stabilized by a second shell of 10 highly conserved residues principally by an extensive network of hydrogen bonds.

PubMed: 1740114

実験手法

X-RAY DIFFRACTION (2.2 Å)