PDBsum entry 6hu4

Virus like particle

PDB id: 6hu4

Contents

Protein chains

151 a.a.

Ligands

SER-GLN-CYS ×4

PDB id:

6hu4

Name:

Virus like particle

Title:

F97l hepatitis b core protein capsid

Structure:

Capsid protein. Chain: b, a, c, d, e, f, g, h. Synonym: core antigen,core protein,hbcag,p21.5. Engineered: yes. Other_details: hepatitis b core protein premature envelopment mutant f97l

Source:

Hepatitis b virus. Organism_taxid: 10407. Expressed in: escherichia coli. Expression_system_taxid: 562

Authors:

B.Bottcher,M.Nassal

Key ref:

B.Böttcher and M.Nassal (2018). Structure of Mutant Hepatitis B Core Protein Capsids with Premature Secretion Phenotype. J Mol Biol, 430, 4941-4954. PubMed id: 30539760 DOI: 10.1016/j.jmb.2018.10.018

Date:

05-Oct-18 Release date: 26-Dec-18

Protein chains

P03146  (CAPSD_HBVD3) -  Capsid protein from Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979)

Seq: 183 a.a.

Struc: 151 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.jmb.2018.10.018

J Mol Biol 430:4941-4954 (2018)

PubMed id: 30539760

Structure of Mutant Hepatitis B Core Protein Capsids with Premature Secretion Phenotype.

B.Böttcher, M.Nassal.

ABSTRACT

Hepatitis B virus is a major human pathogen that consists of a viral genome surrounded by an icosahedrally ordered core protein and a polymorphic, lipidic envelope that is densely packed with surface proteins. A point mutation in the core protein in which a phenylalanine at position 97 is exchanged for a smaller leucine leads to premature envelopment of the capsid before the genome maturation is fully completed. We have used electron cryo-microscopy and image processing to investigate how the point mutation affects the structure of the capsid at 2.6- to 2.8 Å-resolution. We found that in the mutant the smaller side chain at position 97 is displaced, increasing the size of an adjacent pocket in the center of the spikes of the capsid. In the mutant, this pocket is filled with an unknown density. Phosphorylation of serine residues in the unresolved C-terminal domain of the mutant leaves the structure of the ordered capsid largely unchanged. However, we were able to resolve several previously unresolved residues downstream of proline 144 that precede the phosphorylation-sites. These residues pack against the neighboring subunits and increase the inter-dimer contact suggesting that the C-termini play an important role in capsid stabilization and provide a much larger interaction interface than previously observed.