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Publication Abstract from PubMed

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 A 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.

Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin.,Meyer A, Rypniewski W, Szymanski M, Voelter W, Barciszewski J, Betzel C Biochim Biophys Acta. 2008 Nov;1784(11):1590-5. Epub 2008 Jul 31. PMID:18718563^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.