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PDBsum entry 5jbg

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protein dna_rna ligands metals links
Immune system PDB id
5jbg

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
661 a.a.
DNA/RNA
Ligands
ADP
ALF
SO4 ×5
Metals
_ZN
_MG
Waters ×268
PDB id:
5jbg
Name: Immune system
Title: Crystal structure of chicken lgp2 with 5'ppp 26-mer hairpin RNA with 3' gg overhang and adp-alf4-mg2+ at 2.0 a resolution.
Structure: Lgp2. Chain: a. Engineered: yes. Mutation: yes. RNA (5'- r( Gppp Gp Ap Gp Cp Gp Up Gp Cp Cp Gp Gp Gp Cp Ap Cp Gp Cp Up Cp Cp G p G)-3'). Chain: x. Engineered: yes.
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta 2. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
2.00Å     R-factor:   0.219     R-free:   0.255
Authors: S.Cusack,E.Uchikawa
Key ref: E.Uchikawa et al. (2016). Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5. Mol Cell, 62, 586-602. PubMed id: 27203181 DOI: 10.1016/j.molcel.2016.04.021
Date:
13-Apr-16     Release date:   01-Jun-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
G0YYQ5  (G0YYQ5_CHICK) -  RNA helicase from Gallus gallus
Seq:
Struc:
 
Seq:
Struc:
674 a.a.
661 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

DNA/RNA chain
  GTP-G-A-G-C-G-U-G-C-C-G-G-G-C-A-C-G-C-U-C-C-G-G 23 bases

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
=
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.molcel.2016.04.021 Mol Cell 62:586-602 (2016)
PubMed id: 27203181  
 
 
Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5.
E.Uchikawa, M.Lethier, H.Malet, J.Brunel, D.Gerlier, S.Cusack.
 
  ABSTRACT  
 
RIG-I and MDA5 sense virus-derived short 5'ppp blunt-ended or long dsRNA, respectively, causing interferon production. Non-signaling LGP2 appears to positively and negatively regulate MDA5 and RIG-I signaling, respectively. Co-crystal structures of chicken (ch) LGP2 with dsRNA display a fully or semi-closed conformation depending on the presence or absence of nucleotide. LGP2 caps blunt, 3' or 5' overhang dsRNA ends with 1 bp longer overall footprint than RIG-I. Structures of 1:1 and 2:1 complexes of chMDA5 with short dsRNA reveal head-to-head packing rather than the polar head-to-tail orientation described for long filaments. chLGP2 and chMDA5 make filaments with a similar axial repeat, although less co-operatively for chLGP2. Overall, LGP2 resembles a chimera combining a MDA5-like helicase domain and RIG-I like CTD supporting both stem and end binding. Functionally, RNA binding is required for LGP2-mediated enhancement of MDA5 activation. We propose that LGP2 end-binding may promote nucleation of MDA5 oligomerization on dsRNA.
 

 

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