1EOQ

ROUS SARCOMA VIRUS CAPSID PROTEIN: C-TERMINAL DOMAIN


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Submitted: 

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This is version 1.5 of the entry. See complete history


Literature

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

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

(2000) Structure 8: 617-628

  • DOI: https://doi.org/10.1016/s0969-2126(00)00148-9
  • Primary Citation of Related Structures:  
    1EM9, 1EOQ

  • PubMed Abstract: 

    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. 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. 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.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GAG POLYPROTEIN CAPSID PROTEIN P2796Rous sarcoma virus - Prague CMutation(s): 0 
UniProt
Find proteins for P03322 (Rous sarcoma virus subgroup C (strain Prague))
Explore P03322 
Go to UniProtKB:  P03322
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03322
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Submitted: 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-08-02
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-06-05
    Changes: Data collection, Derived calculations, Structure summary
  • Version 1.4: 2022-12-21
    Changes: Database references
  • Version 1.5: 2024-05-22
    Changes: Data collection