PDBsum entry: 1eoq

Viral protein

PDB id: 1eoq

Contents

Protein chain

77 a.a. *

* Residue conservation analysis

PDB id:

1eoq

Name:

Viral protein

Title:

Rous sarcoma virus capsid protein: c-terminal domain

Structure:

Gag polyprotein capsid protein p27. Chain: a. Fragment: c-terminal domain. Engineered: yes

Source:

Rous sarcoma virus - praguE C. Organism_taxid: 11888. Strain: praguE C. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

1 models

Authors:

R.L.Kingston,T.Fitzon-Ostendorp,E.Z.Eisenmesser,G.W.Schatz, V.M.Vogt,C.B.Post,M.G.Rossman

Key ref:

R.L.Kingston et al. (2000). Structure and self-association of the Rous sarcoma virus capsid protein. Structure, 8, 617-628. PubMed id: 10873863 DOI: 10.1016/S0969-2126(00)00148-9

Date:

23-Mar-00 Release date: 02-Aug-00

Protein chain

P03322  (GAG_RSVP) -  Gag-Pro polyprotein

Seq: 701 a.a.

Struc: 77 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Biological process: viral reproduction (1 term)

DOI no: 10.1016/S0969-2126(00)00148-9

Structure 8:617-628 (2000)

PubMed id: 10873863

Structure and self-association of the Rous sarcoma virus capsid protein.

R.L.Kingston, T.Fitzon-Ostendorp, E.Z.Eisenmesser, G.W.Schatz, V.M.Vogt, C.B.Post, M.G.Rossmann.

ABSTRACT

BACKGROUND: The capsid protein (CA) of retroviruses, such as Rous sarcoma virus (RSV), consists of two independently folded domains. CA functions as part of a polyprotein during particle assembly and budding and, in addition, forms a shell encapsidating the genomic RNA in the mature, infectious virus. RESULTS: The structures of the N- and C-terminal domains of RSV CA have been determined by X-ray crystallography and solution nuclear magnetic resonance (NMR) spectroscopy, respectively. The N-terminal domain comprises seven alpha helices and a short beta hairpin at the N terminus. The N-terminal domain associates through a small, tightly packed, twofold symmetric interface within the crystal, different from those previously described for other retroviral CAs. The C-terminal domain is a compact bundle of four alpha helices, although the last few residues are disordered. In dilute solution, RSV CA is predominantly monomeric. We show, however, using electron microscopy, that intact RSV CA can assemble in vitro to form both tubular structures constructed from toroidal oligomers and planar monolayers. Both modes of assembly occur under similar solution conditions, and both sheets and tubes exhibit long-range order. CONCLUSIONS: The tertiary structure of CA is conserved across the major retroviral genera, yet sequence variations are sufficient to cause change in associative behavior. CA forms the exterior shell of the viral core in all mature retroviruses. However, the core morphology differs between viruses. Consistent with this observation, we find that the capsid proteins of RSV and human immunodeficiency virus type 1 exhibit different associative behavior in dilute solution and assemble in vitro into different structures.

Selected figure(s)

Figure 1.
Figure 1. The N-terminal domain of the retroviral capsid protein. (a) RSV, (b) HIV-1. The b hairpin is shown in detail, in an orientation that is slightly different from that of the whole domain. The boundaries of the helices within the N-terminal domain of RSV CA are: helix 1, 15-30; 2, 33-44; 3, 49-61; 4, 62-87; 5, 102-107; 6, 116-124; 7, 125-147. Helix definitions incorporate the N- and C-terminal capping residues. Coordinates for the N-terminal domain of HIV-1 CA were taken from the X-ray structure of the molecule in complex with cyclophilin A [3]. The program Ribbons 2.0 [50] was used in the preparation of the figure.

The above figure is reprinted by permission from Cell Press: Structure (2000, 8, 617-628) copyright 2000.

Figure was selected by an automated process.