1sva

OverviewOverview

BACKGROUND: The structure of simian virus 40 (SV40), previously determined, at 3.8 degree resolution, shows how its pentameric VP1 assembly units are, tied together by extended C-terminal arms. In order to define more, precisely the possible assembly mechanisms, we have refined the structure, at 3.1 degree resolution. RESULTS: New data from a high-intensity, synchrotron source have been used for phase extension by electron-density, averaging and refinement, exploiting only the strict 5-fold, non-crystallographic symmetry for the real-space averaging steps. The, accurate model enables us to study important structural features of the, virus particle in detail. The remarkably invariant core of the VP1, pentamer bears the docking sites for the C-terminal arms from other, pentamers. These contacts are the principal way in which pentameric, assembly units are linked together in the capsid. Only at the interface, between five-coordinated and six-coordinated pentamers do the pentamer, cores appear to interact strongly. There are two cation-binding sites per, VP1 monomer, seen in a soaking experiment with gadolinium nitrate. These, sites are quite close to each other at the interfaces between pentamers., CONCLUSION: We propose that the contact between five-coordinated and, six-coordinated pentamers may help to generate a six-pentamer nucleus, with which further pentamers can assemble to generate the complete, particle. Calcium ions probably stabilize the structure of the assembled, particle, rather than direct its assembly.

About this StructureAbout this Structure

1SVA is a Single protein structure of sequence from Simian virus 40. The following page contains interesting information on the relation of 1SVA with [Simian Virus 40]. Full crystallographic information is available from OCA.

ReferenceReference

The structure of simian virus 40 refined at 3.1 A resolution., Stehle T, Gamblin SJ, Yan Y, Harrison SC, Structure. 1996 Feb 15;4(2):165-82. PMID:8805523

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