spacer
spacer

PDBsum entry 4gnk

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Gtp-binding protein/hydrolase PDB id
4gnk
Jmol
Contents
Protein chains
337 a.a.
769 a.a.
235 a.a.
Ligands
GDP-ALF ×2
Metals
_MG ×2
_CA ×2
Waters ×6
PDB id:
4gnk
Name: Gtp-binding protein/hydrolase
Title: Crystal structure of galphaq in complex with full-length hum plcbeta3
Structure: Guanine nucleotide-binding protein g(q) subunit a chain: a, c. Fragment: unp residues 7-359. Synonym: guanine nucleotide-binding protein alpha-q. Engineered: yes. 1-phosphatidylinositol 4,5-bisphosphate phosphodi beta-3. Chain: b, d. Fragment: unp residues 10-1234.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Gene: g alpha q, gnaq. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Homo sapiens. Human. Organism_taxid: 9606.
Resolution:
4.00Å     R-factor:   0.216     R-free:   0.255
Authors: A.M.Lyon,J.J.G.Tesmer
Key ref: A.M.Lyon et al. (2013). Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. Nat Struct Mol Biol, 20, 355-362. PubMed id: 23377541 DOI: 10.1038/nsmb.2497
Date:
17-Aug-12     Release date:   06-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21279  (GNAQ_MOUSE) -  Guanine nucleotide-binding protein G(q) subunit alpha
Seq:
Struc:
359 a.a.
337 a.a.
Protein chains
Pfam   ArchSchema ?
Q01970  (PLCB3_HUMAN) -  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1234 a.a.
769 a.a.
Protein chain
Pfam   ArchSchema ?
Q01970  (PLCB3_HUMAN) -  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1234 a.a.
235 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains B, D, E: E.C.3.1.4.11  - Phosphoinositide phospholipase C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
myo-Inositol Phosphate Metabolism
      Reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
+ H(2)O
= 1D-myo-inositol 1,4,5-trisphosphate
+ diacylglycerol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   10 terms 
  Biological process     regulation of catenin import into nucleus   27 terms 
  Biochemical function     nucleotide binding     17 terms  

 

 
    reference    
 
 
DOI no: 10.1038/nsmb.2497 Nat Struct Mol Biol 20:355-362 (2013)
PubMed id: 23377541  
 
 
Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain.
A.M.Lyon, S.Dutta, C.A.Boguth, G.Skiniotis, J.J.Tesmer.
 
  ABSTRACT  
 
Phospholipase C-β (PLCβ) is directly activated by Gαq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCβ3 in complex with mouse Gαq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments with structural similarity to membrane-binding bin-amphiphysin-Rvs (BAR) domains. Sequence conservation of the distal CTD suggests putative membrane and protein interaction sites, the latter of which bind the N-terminal helix of Gαq in both the crystal structure and cryo-EM reconstructions. Functional analysis suggests that the distal CTD has roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis.