1LVM

CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT

1LVM の概要

• エントリーDOI: 10.2210/pdb1lvm/pdb
• 関連するPDBエントリー: 1LVB
• 分子名称: CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA), OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE, ... (4 entities in total)
• 機能のキーワード: beta barrel, chymotrypsin-type cystein protease, enzyme-peptide complex, viral protein
• 由来する生物種: Tobacco etch virus; 詳細
• 細胞内の位置: Capsid protein: Virion (Potential): P04517 P04517 P04517
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 55269.34

構造登録者

Phan, J.,Zdanov, A.,Evdokimov, A.G.,Tropea, J.E.,Peters III, H.K.,Kapust, R.B.,Li, M.,Wlodawer, A.,Waugh, D.S. (登録日: 2002-05-28, 公開日: 2002-11-27, 最終更新日: 2024-10-30)

主引用文献

Phan, J.,Zdanov, A.,Evdokimov, A.G.,Tropea, J.E.,Peters III, H.K.,Kapust, R.B.,Li, M.,Wlodawer, A.,Waugh, D.S.
Structural basis for the substrate specificity of tobacco etch virus protease.
J.Biol.Chem., 277:50564-50572, 2002

PubMed Abstract: Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.

PubMed: 12377789
DOI: 10.1074/jbc.M207224200

実験手法

X-RAY DIFFRACTION (1.8 Å)