2FYG

Crystal structure of NSP10 from Sars coronavirus

2FYG の概要

• エントリーDOI: 10.2210/pdb2fyg/pdb
• 分子名称: Replicase polyprotein 1ab, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: sars virus polyprotein non-structural protein nsp10, zinc finger, viral protein
• 由来する生物種: SARS coronavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14090.71

構造登録者

Joseph, J.S.,Saikatendu, K.S.,Subramanian, V.,Neuman, B.W.,Brooun, A.,Griffith, M.,Moy, K.,Yadav, M.K.,Velasquez, J.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P. (登録日: 2006-02-07, 公開日: 2006-08-08, 最終更新日: 2024-02-14)

主引用文献

Joseph, J.S.,Saikatendu, K.S.,Subramanian, V.,Neuman, B.W.,Brooun, A.,Griffith, M.,Moy, K.,Yadav, M.K.,Velasquez, J.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.
Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs.
J.Virol., 80:7894-7901, 2006

PubMed Abstract: The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins 1a and 1ab, which are cleaved to generate 16 "nonstructural" proteins, nsp1 to nsp16, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 A as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular beta-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn2+ ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn2+-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.

PubMed: 16873246
DOI: 10.1128/JVI.00467-06

実験手法

X-RAY DIFFRACTION (1.8 Å)