2R9K

Crystal Structure of Misteltoe Lectin I in Complex with Phloretamide

Summary for 2R9K

• Entry DOI: 10.2210/pdb2r9k/pdb
• Related: 1M2T
• Descriptor: Beta-galactoside-specific lectin 1, Beta-galactoside-specific lectin 1 chain B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(4-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: ml-i, phloretamide, viscum album, 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: 58651.51

Authors

Meyer, A.,Rypniewski, W.,Celewicz, L.,Erdmann, V.A.,Voelter, W.,Betzel, C. (deposition date: 2007-09-13, release date: 2007-10-30, Last modification date: 2023-08-30)

Primary citation

Meyer, A.,Rypniewski, W.,Celewicz, L.,Erdmann, V.A.,Voelter, W.,Singh, T.P.,Genov, N.,Barciszewski, J.,Betzel, C.h.
The mistletoe lectin I--phloretamide structure reveals a new function of plant lectins.
Biochem.Biophys.Res.Commun., 364:195-200, 2007

PubMed Abstract: The X-ray structure at 2.7A resolution of the complex between the European mistletoe lectin I (Viscum album, ML-I) and the plant growth hormone, 3-(p-hydroxyphenyl)-propionic acid amide (phloretamide, PA) from xylem sap has revealed the binding of PA at the so far undescribed hydrophobic cavity located between the two subunits of this ribosome-inhibiting protein. No such cavity is observed in related lectins. The binding of PA is achieved through interactions with the non-conserved residues Val228A, Leu230A, Arg388B, and the C-terminal Pro510B. It is conceivable that binding of PA to ML-I is part of a defence mechanism of the parasite against the host, whereby the parasite prevents the growth hormone of the host from interfering with its own regulatory system. The specific binding of PA to ML-I indicates that heterodimeric RIPs are multifunctional proteins whose functions in the cell have not yet been fully recognized and analyzed.

PubMed: 17937929
DOI: 10.1016/j.bbrc.2007.09.113

Experimental method

X-RAY DIFFRACTION (2.7 Å)