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Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album

2011; Elsevier BV; Volume: 1824; Issue: 2 Linguagem: Inglês

10.1016/j.bbapap.2011.10.013

1878-1454

P.H. Malecki, W. Rypniewski, M. Szymański, Jan Barciszewski, Arne Meyer,

Plant Parasitism and Resistance

The crystal structure of the ribosome inhibiting protein Mistletoe Lectin I (ML-I) derived from the European mistletoe, Viscum album, in complex with kinetin has been refined at 2.7 Å resolution. Suitably large crystals of ML-I were obtained applying the counter diffusion method using the Gel Tube R Crystallization Kit (GT-R) on board the Russian Service Module on the international space station ISS within the GCF mission No. 6, arranged by the Japanese aerospace exploration agency (JAXA). Hexagonal bi-pyramidal crystals were grown during three months under microgravity. Before data collection the crystals were soaked in a saturated solution of kinetin and diffraction data to 2.7 Å were collected using synchrotron radiation and cryogenic techniques. The atomic model was refined and revealed a single kinetin molecule in the ribosome inactivation site of ML-I. The complex demonstrates the feasibility of mistletoe to bind plant hormones out of the host regulation system as part of a self protection mechanism.