PDBsum entry 4ph0

Viral protein

PDB id

4ph0

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Contents

			Protein chains

					201 a.a.


					188 a.a.

PDB id:

4ph0

Links

Name:

Viral protein

Title:

Capsid protein from bovine leukemia virus

Structure:

Blv capsid. Chain: a, b, c, d, e, f. Fragment: unp residues 110-324. Engineered: yes

Source:

Bovine leukemia virus. Blv. Organism_taxid: 11901. Gene: gag-pro-pol. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.75Å

R-factor:

0.187

R-free:

0.221

Authors:

F.Trajtenberg,G.Obal,O.Pritsch,A.Buschiazzo

Key ref:

G.Obal et al. (2015). STRUCTURAL VIROLOGY. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography. Science, 349, 95-98. PubMed id: 26044299 DOI: 10.1126/science.aaa5182

Date:

03-May-14

Release date:

10-Jun-15

PROCHECK

	Headers

	References

Protein chains

A7KWZ1 (A7KWZ1_BLV) - Gag-Pro-Pol polyprotein from Bovine leukemia virus

Seq: Struc:

Seq: Struc:

Seq: Struc:					1417 a.a. 201 a.a.

Protein chain

A7KWZ1 (A7KWZ1_BLV) - Gag-Pro-Pol polyprotein from Bovine leukemia virus

Seq: Struc:

Seq: Struc:

Seq: Struc:					1417 a.a. 188 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1126/science.aaa5182	Science 349:95-98 (2015)
PubMed id: 26044299

STRUCTURAL VIROLOGY. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography.
G.Obal, F.Trajtenberg, F.Carrión, L.Tomé, N.Larrieux, X.Zhang, O.Pritsch, A.Buschiazzo.

ABSTRACT

Retroviruses depend on self-assembly of their capsid proteins (core particle) to yield infectious mature virions. Despite the essential role of the retroviral core, its high polymorphism has hindered high-resolution structural analyses. Here, we report the x-ray structure of the native capsid (CA) protein from bovine leukemia virus. CA is organized as hexamers that deviate substantially from sixfold symmetry, yet adjust to make two-dimensional pseudohexagonal arrays that mimic mature retroviral cores. Intra- and interhexameric quasi-equivalent contacts are uncovered, with flexible trimeric lateral contacts among hexamers, yet preserving very similar dimeric interfaces making the lattice. The conformation of each capsid subunit in the hexamer is therefore dictated by long-range interactions, revealing how the hexamers can also assemble into closed core particles, a relevant feature of retrovirus biology.