2CME

The crystal structure of SARS coronavirus ORF-9b protein

2CME の概要

• エントリーDOI: 10.2210/pdb2cme/pdb
• 分子名称: HYPOTHETICAL PROTEIN 5, DECANE, ... (6 entities in total)
• 機能のキーワード: alternative open reading frame, lipid-binding, virus assembly, hypothetical protein
• 由来する生物種: HUMAN SARS CORONAVIRUS (SARS); 詳細
• 細胞内の位置: Host cytoplasmic vesicle membrane; Peripheral membrane protein: P59636 P59636 P59636 P59636
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 68631.35

構造登録者

Meier, C.,Aricescu, A.R.,Assenberg, R.,Aplin, R.T.,Gilbert, R.J.C.,Grimes, J.M.,Stuart, D.I. (登録日: 2006-05-06, 公開日: 2006-07-19, 最終更新日: 2024-05-08)

主引用文献

Meier, C.,Aricescu, A.R.,Assenberg, R.,Aplin, R.T.,Gilbert, R.J.C.,Grimes, J.M.,Stuart, D.I.
The Crystal Structure of Orf-9B, a Lipid Binding Protein from the Sars Coronavirus.
Structure, 14:1157-, 2006

PubMed Abstract: To achieve the greatest output from their limited genomes, viruses frequently make use of alternative open reading frames, in which translation is initiated from a start codon within an existing gene and, being out of frame, gives rise to a distinct protein product. These alternative protein products are, as yet, poorly characterized structurally. Here we report the crystal structure of ORF-9b, an alternative open reading frame within the nucleocapsid (N) gene from the SARS coronavirus. The protein has a novel fold, a dimeric tent-like beta structure with an amphipathic surface, and a central hydrophobic cavity that binds lipid molecules. This cavity is likely to be involved in membrane attachment and, in mammalian cells, ORF-9b associates with intracellular vesicles, consistent with a role in the assembly of the virion. Analysis of ORF-9b and other overlapping genes suggests that they provide snapshots of the early evolution of novel protein folds.

PubMed: 16843897
DOI: 10.1016/J.STR.2006.05.012

実験手法

X-RAY DIFFRACTION (2.8 Å)