3FQQ

Crystal structure of a novel dimeric form of HCV NS5A domain I protein

3FQQ の概要

• エントリーDOI: 10.2210/pdb3fqq/pdb
• 関連するPDBエントリー: 1ZH1 2FQM
• 分子名称: Non-structural protein 5A, ZINC ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: hcv, ns5a, domain i, phosphoprotein, rna-binding, metal binding protein
• 由来する生物種: Hepatitis C virus (isolate Con1) (HCV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39627.62

構造登録者

Love, R.A. (登録日: 2009-01-07, 公開日: 2009-03-24, 最終更新日: 2023-09-06)

主引用文献

Love, R.A.,Brodsky, O.,Hickey, M.J.,Wells, P.A.,Cronin, C.N.
Crystal structure of a novel dimeric form of NS5A domain I protein from hepatitis C virus
J.Virol., 83:4395-4403, 2009

PubMed Abstract: A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly.

PubMed: 19244328
DOI: 10.1128/JVI.02352-08

実験手法

X-RAY DIFFRACTION (2.2 Å)