By the same authors

From the same journal

A TIM BARREL PROTEIN WITHOUT ENZYMATIC ACTIVITY? CRYSTAL STRUCTURE OF NARBONIN AT 1.8 Å RESOLUTION

Research output: Contribution to journalArticle

Author(s)

  • M HENNIG
  • B SCHLESIER
  • Z DAUTER
  • S PFEFFER
  • C BETZEL
  • W E HOHNE
  • K S WILSON

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 13 Jul 1992
Issue number1
Volume306
Number of pages5
Pages (from-to)80-84
Original languageEnglish

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.

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