A TIM barrel protein without enzymatic activity? Crystal-structure of narbonin at 1.8 Å resolution

The major protein component in seeds is storage protein. These have no known enzymatic activity and act to provide amino acids as a source of metabolites in the developing seedling. We report here the first three dimensional crystal structure of a seed storage globulin at high resolution. The molecu...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:FEBS letters 1992-07, Vol.306 (1), p.80-84
Hauptverfasser: Hennig, Michael, Schlesier, Bernhard, Dauter, Zbigniew, Pfeffer, Sabine, Betzel, Christian, Höhne, Wolfgang E., Wilson, Keith S.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The major protein component in seeds is storage protein. These have no known enzymatic activity and act to provide amino acids as a source of metabolites in the developing seedling. We report here the first three dimensional crystal structure of a seed storage globulin at high resolution. The molecule of the 2S globulin, narbonin, from Vicia narbonensis L. consists of an eight-stranded parallel α/gb barrel structure similar to that observed in triose phosphate isomerase (TIM). Narbonin is the first protein with this topology possessing no known enzymatic activity. Because of the lack of sequence information most of the primary structure was determined directly from the electron density.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(92)80842-5