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PDBsum entry 2r9k

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2r9k
Jmol
Contents
Protein chains
248 a.a. *
262 a.a. *
Ligands
NAG ×4
SO4 ×4
GOL ×4
SGI
NAG-NAG
Metals
_CL
Waters ×72
* Residue conservation analysis
PDB id:
2r9k
Name: Hydrolase
Title: Crystal structure of misteltoe lectin i in complex with phlo
Structure: Beta-galactoside-specific lectin 1. Chain: a. Fragment: beta-galactoside-specific lectin 1 chain a isofor residues 34-287. Synonym: beta-galactoside-specific lectin i, viscumin. Engineered: yes. Beta-galactoside-specific lectin 1. Chain: b. Fragment: beta-galactoside-specific lectin 1 chain b, unp r
Source: Viscum album. European mistletoe. Organism_taxid: 3972. Organism_taxid: 3972
Resolution:
2.70Å     R-factor:   0.228     R-free:   0.267
Authors: A.Meyer,W.Rypniewski,L.Celewicz,V.A.Erdmann,W.Voelter,C.Betz
Key ref: A.Meyer et al. (2007). The mistletoe lectin I--phloretamide structure reveals a new function of plant lectins. Biochem Biophys Res Commun, 364, 195-200. PubMed id: 17937929 DOI: 10.1016/j.bbrc.2007.09.113
Date:
13-Sep-07     Release date:   30-Oct-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P81446  (ML1_VISAL) -  Beta-galactoside-specific lectin 1
Seq:
Struc:
 
Seq:
Struc:
564 a.a.
248 a.a.*
Protein chain
Pfam   ArchSchema ?
P81446  (ML1_VISAL) -  Beta-galactoside-specific lectin 1
Seq:
Struc:
 
Seq:
Struc:
564 a.a.
262 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 50 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.3.2.2.22  - 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.bbrc.2007.09.113 Biochem Biophys Res Commun 364:195-200 (2007)
PubMed id: 17937929  
 
 
The mistletoe lectin I--phloretamide structure reveals a new function of plant lectins.
A.Meyer, W.Rypniewski, L.Celewicz, V.A.Erdmann, W.Voelter, T.P.Singh, N.Genov, J.Barciszewski, C.h.Betzel.
 
  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.