3J2V

CryoEM structure of HBV core

3J2V の概要

• エントリーDOI: 10.2210/pdb3j2v/pdb
• EMDBエントリー: 2278
• 分子名称: PreC/core protein (1 entity in total)
• 機能のキーワード: hepatitis b virus core antigen (hbc), no cys61 intermolecular disulfide bond, virus
• 由来する生物種: Hepatitis B virus (HBV)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 85593.86

構造登録者

Yu, X.,Jin, L.,Jih, J.,Shih, C.,Zhou, Z.H. (登録日: 2013-01-11, 公開日: 2013-10-02, 最終更新日: 2024-02-21)

主引用文献

Yu, X.,Jin, L.,Jih, J.,Shih, C.,Zhou, Z.H.
3.5 angstrom cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein.
Plos One, 8:e69729-e69729, 2013

PubMed Abstract: The capsid shell of infectious hepatitis B virus (HBV) is composed of 240 copies of a single protein called HBV core antigen (HBc). An atomic model of a core assembled from truncated HBc was determined previously by X-ray crystallography. In an attempt to obtain atomic structural information of HBV core in a near native, non-crystalline environment, we reconstructed a 3.5Å-resolution structure of a recombinant core assembled from full-length HBc by cryo electron microscopy (cryoEM) and derived an atomic model. The structure shows that the 240 molecules of full-length HBc form a core with two layers. The outer layer, composed of the N-terminal assembly domain, is similar to the crystal structure of the truncated HBc, but has three differences. First, unlike the crystal structure, our cryoEM structure shows no disulfide bond between the Cys61 residues of the two subunits within the dimer building block, indicating such bond is not required for core formation. Second, our cryoEM structure reveals up to four more residues in the linker region (amino acids 140-149). Third, the loops in the cryoEM structures containing this linker region in subunits B and C are oriented differently (~30° and ~90°) from their counterparts in the crystal structure. The inner layer, composed of the C-terminal arginine-rich domain (ARD) and the ARD-bound RNAs, is partially-ordered and connected with the outer layer through linkers positioned around the two-fold axes. Weak densities emanate from the rims of positively charged channels through the icosahedral three-fold and local three-fold axes. We attribute these densities to the exposed portions of some ARDs, thus explaining ARD's accessibility by proteases and antibodies. Our data supports a role of ARD in mediating communication between inside and outside of the core during HBV maturation and envelopment.

PubMed: 24039702
DOI: 10.1371/journal.pone.0069729

実験手法

ELECTRON MICROSCOPY (3.5 Å)