2r9k
From Proteopedia
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , and | ||||||
| Ligands: | , , , , | ||||||
| Related: | 1M2T
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Misteltoe Lectin I in Complex with Phloretamide
Overview
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.
About this Structure
2R9K is a Protein complex structure of sequences from Viscum album. Full crystallographic information is available from OCA.
Reference
The mistletoe lectin I--phloretamide structure reveals a new function of plant lectins., Meyer A, Rypniewski W, Celewicz L, Erdmann VA, Voelter W, Singh TP, Genov N, Barciszewski J, Betzel Ch, Biochem Biophys Res Commun. 2007 Dec 14;364(2):195-200. Epub 2007 Oct 5. PMID:17937929
Page seeded by OCA on Mon Mar 31 04:57:51 2008
