Summary for 3D7W
| Entry DOI | 10.2210/pdb3d7w/pdb |
| Related | 1M2T 2R9K |
| Descriptor | Beta-galactoside-specific lectin 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | mistletoe lectin i, cytokinin, zeatin, plant hormones, microgravity, glycoprotein, hydrolase, lectin, plant defense, protein synthesis inhibitor, toxin |
| Biological source | Viscum album (European mistletoe) More |
| Total number of polymer chains | 2 |
| Total formula weight | 59027.58 |
| Authors | Meyer, A.,Rypniewski, W.,Szymanski, M.,Voelter, W.,Barciszewski, J.,Betzel, C. (deposition date: 2008-05-22, release date: 2008-06-17, Last modification date: 2024-10-30) |
| Primary citation | Meyer, A.,Rypniewski, W.,Szymanski, M.,Voelter, W.,Barciszewski, J.,Betzel, C. Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin Biochim.Biophys.Acta, 1784:1590-1595, 2008 Cited by PubMed Abstract: 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. PubMed: 18718563DOI: 10.1016/j.bbapap.2008.07.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
Download full validation report
