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

FEBS Letters

Dauter, Zbigniew³  Pfeffer, Sabine³  Betzel, Christian³  Hennig, Michael³  Wilson, Keith S.³  Schlesier, Bernhard²  Höhne, Wolfgang E.¹ 

[1] Institut für Biochemie der Humboldt-Universität zu Berlin, Hessische Str. 3-4, O-1040 Berlin, Germany;Institut für Pflanzengenetik und Kulturpflanzenforschung, Correnstrasse 3, O-4325 Gatersleben, Germany;European Molecular Biology Laboratory (EMBL) c/o DESY, Notkestrasse 85, W-2000 Hamburg 52, Germany

关键词: Seed storage protein;    Vicia narbonensis;    X-ray structure;    TIM barrel;    Primary structure;   

DOI  :  10.1016/0014-5793(92)80842-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown