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

Important note: Information in this article was accurate in 2000. The state of the art may have changed since the publication date.

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

Structure Fold Des. 2000 Jun 15;8(6):617-28. Unique Identifier : AIDSLINE PDB/1EOQ
Kingston RL; Fitzon-Ostendorp T; Eisenmesser EZ; Schatz GW; Vogt VM; Post CB; Rossmann MG; Department of Biological Sciences, Purdue University, West; Lafayette, IN 47907, USA.

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.

Keywords: JOURNAL ARTICLE Capsid/*CHEMISTRY/ULTRASTRUCTURE Crystallography, X-Ray Human Microscopy, Electron Models, Molecular Nuclear Magnetic Resonance Protein Structure, Secondary Protein Structure, Tertiary Sarcoma Viruses, Avian/*CHEMISTRY/GROWTH & DEVELOPMENT/ ULTRASTRUCTURE Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S.

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A00B1156

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