Post-translational modification of barley LTP1b: the lipid adduct lies in the hydrophobic cavity and alters the protein dynamics.
NMR techniques have been used to characterise the effects of a lipid-like post-translational modification on barley lipid transfer protein (LTP1b). NMR chemical shift data indicate that the lipid-like molecule lies in the hydrophobic cavity of LTP1b, with Tyr 79 being displaced to accommodate the ligand in the cavity. The modified protein has a reduced level of backbone amide hydrogen exchange protection, presumably reflecting increased dynamics in the protein. This may result from a loosening of the protein structure and may explain the enhanced surface properties observed for LTP1b.
Wijesinha-Bettoni
Ramani
R
Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, UK.
Gao
Chunli
C
Jenkins
John A
JA
Mackie
Alan R
AR
Wilde
Peter J
PJ
Mills
E N Clare
EN
Smith
Lorna J
LJ
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D041961:Deuterium Exchange Measurement; D050556:Fatty Acid-Binding Proteins; D001467:Hordeum / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D013499:Surface Properties
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D008055:Lipids; C422456:Ltp1 protein, barley