Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins

Mathilde Hauge Lerche, Flemming M. Poulsen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The structure of a nonspecific lipid transfer protein from barley (ns-LTPbarley) in complex with palmitate has been determined by NMR spectroscopy. The structure has been compared to the structure of ns-LTPbarley in the absence of palmitate, to the structure of ns-LTPbarley in complex with palmitoyl coenzyme A, to the structure ofns-LTPmaize in its free form, and to the maize protein complexed with palmitate. Binding of palmitate only affects the structure of ns-LTPbarley moderately in contrast to the binding of palmitoyl coenzyme A, which leads to a considerable expansion of the protein. The modes of binding palmitate to the maize and barley protein are different. Although in neither case there are major conformational changes in the protein, the orientation of the palmitate in the two proteins is exactly opposite.
Original languageEnglish
JournalProtein Science
Volume7
Issue number12
Pages (from-to)2490-2498
ISSN0961-8368
DOIs
Publication statusPublished - 1998
Externally publishedYes

Keywords

  • Barley lipid transfer protein
  • Binding
  • Complex
  • Cutin synthesis
  • NMR spectroscopy
  • Solution structure

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