5GJB

Zika virus NS3 helicase in complex with ssRNA

5GJB の概要

• エントリーDOI: 10.2210/pdb5gjb/pdb
• 関連するPDBエントリー: 5GJC
• 分子名称: NS3 helicase, RNA (5'-R(*AP*GP*AP*UP*CP*AP*A)-3') (3 entities in total)
• 機能のキーワード: zika virus, helicase, rna, hydrolase-rna complex, hydrolase/rna
• 由来する生物種: Zika virus (strain Mr 766) (ZIKV); 詳細
• 細胞内の位置: Virion membrane ; Multi-pass membrane protein : A0A142DS38
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52799.03

構造登録者

Tian, H.L.,Ji, X.Y.,Yang, X.Y.,Zhang, Z.X.,Lu, Z.K.,Yang, K.L.,Chen, C.,Zhao, Q.,Chi, H.,Mu, Z.Y.,Xie, W.,Wang, Z.F.,Lou, H.Q.,Yang, H.T.,Rao, Z.H. (登録日: 2016-06-28, 公開日: 2016-07-20, 最終更新日: 2023-11-08)

主引用文献

Tian, H.L.,Ji, X.Y.,Yang, X.Y.,Zhang, Z.X.,Lu, Z.K.,Yang, K.L.,Chen, C.,Zhao, Q.,Chi, H.,Mu, Z.Y.,Xie, W.,Wang, Z.F.,Lou, H.Q.,Yang, H.T.,Rao, Z.H.
Structural basis of Zika virus helicase in recognizing its substrates
Protein Cell, 7:562-570, 2016

PubMed Abstract: The recent explosive outbreak of Zika virus (ZIKV) infection has been reported in South and Central America and the Caribbean. Neonatal microcephaly associated with ZIKV infection has already caused a public health emergency of international concern. No specific vaccines or drugs are currently available to treat ZIKV infection. The ZIKV helicase, which plays a pivotal role in viral RNA replication, is an attractive target for therapy. We determined the crystal structures of ZIKV helicase-ATP-Mn(2+) and ZIKV helicase-RNA. This is the first structure of any flavivirus helicase bound to ATP. Comparisons with related flavivirus helicases have shown that although the critical P-loop in the active site has variable conformations among different species, it adopts an identical mode to recognize ATP/Mn(2+). The structure of ZIKV helicase-RNA has revealed that upon RNA binding, rotations of the motor domains can cause significant conformational changes. Strikingly, although ZIKV and dengue virus (DENV) apo-helicases share conserved residues for RNA binding, their different manners of motor domain rotations result in distinct individual modes for RNA recognition. It suggests that flavivirus helicases could have evolved a conserved engine to convert chemical energy from nucleoside triphosphate to mechanical energy for RNA unwinding, but different motor domain rotations result in variable RNA recognition modes to adapt to individual viral replication.

PubMed: 27430951
DOI: 10.1007/s13238-016-0293-2

実験手法

X-RAY DIFFRACTION (1.702 Å)