Back to Search Start Over

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

Authors :
Hennig, Michael
Schlesier, Bernhard
Dauter, Zbigniew
Pfeffer, Sabine
Betzel, Christian
Höhne, Wolfgang E.
Wilson, Keith S.
Source :
FEBS Letters; January 1992, Vol. 306 Issue: 1 p80-84, 5p
Publication Year :
1992

Abstract

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 narbonensisL. 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.

Details

Language :
English
ISSN :
00145793
Volume :
306
Issue :
1
Database :
Supplemental Index
Journal :
FEBS Letters
Publication Type :
Periodical
Accession number :
ejs66295007
Full Text :
https://doi.org/10.1016/0014-5793(92)80842-5