BARLEY LIPID
TRANSFER PROTEIN 1 WITH A COVALENTLY ATTACHED LIPID-LIKE MOLECULE
Jitka
Žídková1, Jozef
Hritz2, Michaela Matejková3, Lukáš
Žídek3, Vladimír Sklenář3,
Janette Bobáľová1
1Institute of Analytical Chemistry, Academy
of Sciences of the Czech Republic, v.v.i., Veveří 97, 60200 Brno, Czech Republic
2Department of Pharmacochemistry,
Vrije Universiteit, De Boelelaan 1083, NL-1081 HV Amsterdam, The
Netherlands
3National Centre for Biomolecular Research, Faculty of Science, Masaryk
University, Kotlářská 2, 61137 Brno, Czech
Republic
zidkova@iach.cz
Lipid
transfer protein 1 (LTP1) from barley is a small protein able to transfer
lipids across a membrane in vitro. Its physiological role is not clear, it has been proposed to be involved in cutin synthesis and plant defense mechanism. LTP1 is also
important commercially, as it has an effect on beer foam formation.
Interestingly, LTP1 isolated from barley flour is almost completely covalently
modified with 9-hydroxy-10-oxo-12-Z-octadecenoic acid, bound to Asp 7
via an ester bond. The lipid modification alters physico-chemical
properties of the protein and contributes to its unusual heat stability. An
X-ray structure of the lipid-modified protein (LTP1b) has been published
recently (3GSH.PDB). In our study, we clarify some ambiguities related to the
resolution of the bound lipid in the X-ray structure and present complementary
NMR data illustrating dynamic behavior of the protein. In addition, we describe
a computational protocol used to predict the 3D structure of LTP1b without a knowledge of the X-ray structure, based on a docking
approach.
Acknowledgments
This work
was supported by the Grants 1M0570, MSM0021622413, and LC06030 of the Ministry
of Education, Youth, and Physical Culture of the Czech Republic, and by Grant
AV0Z40310501 of the Academy of Sciences of the Czech Republic.