Tomato bushy stunt virus at 2.9 resolution

The polypeptide chain of a TBSV subunit folds into two domains, connected by a hinge, and a flexibly-linked N-terminal arm. Sixty of the 180 N-terminal arms inter-digitate in groups of three, in an unexpected mode of protein association. The remaining 120 arms are not uniquely positioned with respec...

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Veröffentlicht in:Nature (London) 1978-11, Vol.276 (5686), p.368-373
Hauptverfasser: Harrison, S. C, Olson, A. J, Schutt, C. E, Winkler, F. K, Bricogne, G
Format: Artikel
Sprache:eng
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Zusammenfassung:The polypeptide chain of a TBSV subunit folds into two domains, connected by a hinge, and a flexibly-linked N-terminal arm. Sixty of the 180 N-terminal arms inter-digitate in groups of three, in an unexpected mode of protein association. The remaining 120 arms are not uniquely positioned with respect to the rest of the subunit. RNA is also not uniquely fixed to sites on the major domains.
ISSN:0028-0836
1476-4687
DOI:10.1038/276368a0