PDBsum entry 3d7w

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
249 a.a. *
262 a.a. *
NAG ×4
GOL ×4
SO4 ×2
Waters ×282
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Mistletoe lectin i in complex with zeatin
Structure: Beta-galactoside-specific lectin 1. Chain: a. Fragment: beta-galactoside-specific lectin 1 chain a isofor synonym: beta-galactoside-specific lectin i, viscumin. Beta-galactoside-specific lectin 1. Chain: b. Fragment: beta-galactoside-specific lectin 1 chain b. Synonym: beta-galactoside-specific lectin i, viscumin. Ec:
Source: Viscum album. European mistletoe. Organism_taxid: 3972. Other_details: semiparasitic plant. Other_details: semiparasitic plant
2.49Å     R-factor:   0.184     R-free:   0.224
Authors: A.Meyer,W.Rypniewski,M.Szymanski,W.Voelter,J.Barciszewski,C.
Key ref: A.Meyer et al. (2008). Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin. Biochim Biophys Acta, 1784, 1590-1595. PubMed id: 18718563 DOI: 10.1016/j.bbapap.2008.07.010
22-May-08     Release date:   17-Jun-08    
Supersedes: 3cef
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P81446  (ML1_VISAL) -  Beta-galactoside-specific lectin 1
564 a.a.
249 a.a.*
Protein chain
Pfam   ArchSchema ?
P81446  (ML1_VISAL) -  Beta-galactoside-specific lectin 1
564 a.a.
262 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 47 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.  - rRNA N-glycosylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     negative regulation of translation   1 term 
  Biochemical function     rRNA N-glycosylase activity     1 term  


DOI no: 10.1016/j.bbapap.2008.07.010 Biochim Biophys Acta 1784:1590-1595 (2008)
PubMed id: 18718563  
Structure of mistletoe lectin I from Viscum album in complex with the phytohormone zeatin.
A.Meyer, W.Rypniewski, M.SzymaƄski, W.Voelter, J.Barciszewski, C.Betzel.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20606289 S.Takahashi, T.Tsurumura, K.Aritake, N.Furubayashi, M.Sato, M.Yamanaka, E.Hirota, S.Sano, T.Kobayashi, T.Tanaka, K.Inaka, H.Tanaka, and Y.Urade (2010).
High-quality crystals of human haematopoietic prostaglandin D synthase with novel inhibitors.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 846-850.  
19756298 R.D.Cummings (2009).
The repertoire of glycan determinants in the human glycome.
  Mol Biosyst, 5, 1087-1104.  
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