Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin

The crystal structure of mistletoe lectin I (ML-I) isolated from the European mistletoe Viscum album in complex with the most active phytohormone zeatin has been analyzed and refined to 2.54 Å resolution. X-ray suitable crystals of ML-I were obtained by the counter-diffusion method using the Gel-Tub...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2008-11, Vol.1784 (11), p.1590-1595
Main Authors: Meyer, Arne, Rypniewski, Wojciech, Szymański, Maciej, Voelter, Wolfgang, Barciszewski, Jan, Betzel, Christian
Format: Article
Language:English
Subjects:
Catalytic Domain
Crystallography, X-Ray
Cytokinin
Microgravity
Mistletoe lectin
Models, Biological
Models, Molecular
Multiprotein Complexes - chemistry
Plant Growth Regulators - metabolism
Plant hormone
Protein Binding
Ribosome Inactivating Proteins, Type 2 - chemistry
Ribosome Inactivating Proteins, Type 2 - isolation & purification
Ribosome Inactivating Proteins, Type 2 - metabolism
Toxins, Biological - chemistry
Toxins, Biological - isolation & purification
Toxins, Biological - metabolism
Viscum album - chemistry
Water stress
Zeatin
Zeatin - chemistry
Zeatin - metabolism
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Summary:The crystal structure of mistletoe lectin I (ML-I) isolated from the European mistletoe Viscum album in complex with the most active phytohormone zeatin has been analyzed and refined to 2.54 Å resolution. X-ray suitable crystals of ML-I were obtained by the counter-diffusion method using the Gel-Tube R crystallization kit (GT-R) onboard the Russian Service Module on the international space station ISS. High quality hexagonal bipyramidal crystals were grown during 3 months under microgravity conditions. Selected crystals were soaked in a saturated solution of zeatin and subsequently diffraction data were collected applying synchrotron radiation. A distinct F o- F c electron density has been found inside a binding pocket located in subunit B of ML-I and has been interpreted as a single zeatin molecule. The structure was refined to investigate the zeatin–ML-I interactions in detail. The results demonstrate the ability of mistletoe to protect itself from the host transpiration regulation by absorbing the most active host plant hormones as part of a defense mechanism.
ISSN:1570-9639
0006-3002
1878-1454
DOI:10.1016/j.bbapap.2008.07.010