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PMID: 1628747 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 306 ·No. 1 ·1992-07-13 ·Pages 80-4

Hennig M, Schlesier B, Dauter Z, Pfeffer S, Betzel C, Höhne WE, Wilson KS

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 narbonensis L., consists of an eight-stranded parallel alpha/beta 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.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Computer Simulation Globulins Molecular Sequence Data Plant Proteins/chemistry,metabolism Plant Proteins, Dietary Protein Conformation Triose-Phosphate Isomerase/chemistry,metabolism X-Ray Diffraction
Chemicals
Amino Acids Globulins Plant Proteins Plant Proteins, Dietary narbonin Triose-Phosphate Isomerase
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Hennig M
European Molecular Biology Laboratory (EMBL), Hamburg, Germany.
Schlesier B
Dauter Z
Pfeffer S
Betzel C
Höhne W E
Wilson K S
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1992-07-13
Pages
80-4
Language
English
Region
England
NLM ID
0155157
Subset
IM
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