3O5W

Binding of kinetin in the active site of mistletoe lectin I

Summary for 3O5W

• Entry DOI: 10.2210/pdb3o5w/pdb
• Related: 1M2T 2R9K 3D7W
• Related PRD ID: PRD_900017
• Descriptor: Beta-galactoside-specific lectin 1 chain A isoform 1, Beta-galactoside-specific lectin 1 chain B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: microgravity, cytokinin, active site, viscum album, ribosome inactivating proteins, kinetin, hydrolase
• Biological source: Viscum album (European mistletoe); More
• Total number of polymer chains: 2
• Total formula weight: 59296.90

Authors

Malecki, P.H.,Meyer, A.,Rypniewski, W.,Szymanski, M.,Barciszewski, J.,Betzel, C. (deposition date: 2010-07-28, release date: 2011-09-14, Last modification date: 2024-10-30)

Primary citation

Malecki, P.H.,Rypniewski, W.,Szymanski, M.,Barciszewski, J.,Meyer, A.
Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album.
Biochim.Biophys.Acta, 1824:334-338, 2012

PubMed Abstract: 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 2.7Å 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 2.7Å 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.

PubMed: 22064121
DOI: 10.1016/j.bbapap.2011.10.013

Experimental method

X-RAY DIFFRACTION (2.7 Å)