2GEF

Crystal structure of a Novel viral protease with a serine/lysine catalytic dyad mechanism

2GEF の概要

• エントリーDOI: 10.2210/pdb2gef/pdb
• 分子名称: Protease VP4 (2 entities in total)
• 機能のキーワード: birnavirus, serine/lysine dyad mechamism, lysine general base, hydrolase
• 由来する生物種: Blotched snakehead virus
• 細胞内の位置: Capsid protein VP2: Virion (Potential). Capsid protein VP3: Virion (Potential). Structural peptide 1: Virion (Potential). Structural peptide 2: Virion (Potential). Structural peptide 3: Virion (Potential). Structural peptide 4: Virion (Potential): Q8AZM0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47312.05

構造登録者

Paetzel, M.,Feldman, A.R.,Lee, J.,Delmas, B. (登録日: 2006-03-20, 公開日: 2006-05-02, 最終更新日: 2024-11-20)

主引用文献

Feldman, A.R.,Lee, J.,Delmas, B.,Paetzel, M.
Crystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism
J.Mol.Biol., 358:1378-1389, 2006

PubMed Abstract: The blotched snakehead virus (BSNV), an aquatic birnavirus, encodes a polyprotein (NH2-pVP2-X-VP4-VP3-COOH) that is processed through the proteolytic activity of its own protease (VP4) to liberate itself and the viral proteins pVP2, X and VP3. The protein pVP2 is further processed by VP4 to give rise to the capsid protein VP2 and four structural peptides. We report here the crystal structure of a VP4 protease from BSNV, which displays a catalytic serine/lysine dyad in its active site. This is the first crystal structure of a birnavirus protease and the first crystal structure of a viral protease that utilizes a lysine general base in its catalytic mechanism. The topology of the VP4 substrate binding site is consistent with the enzymes substrate specificity and a nucleophilic attack from the si-face of the substrates scissile bond. Despite low levels of sequence identity, VP4 shows similarities in its active site to other characterized Ser/Lys proteases such as signal peptidase, LexA protease and Lon protease. Together, the structure of VP4 provides insights into the mechanism of a recently characterized clan of serine proteases that utilize a lysine general base and reveals the structure of potential targets for antiviral therapy, especially for other related and economically important viruses, such as infectious bursal disease virus in poultry and infectious pancreatic necrosis virus in aquaculture.

PubMed: 16584747
DOI: 10.1016/j.jmb.2006.02.045

実験手法

X-RAY DIFFRACTION (2.2 Å)