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PDBsum entry 3tw5

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3tw5
Jmol
Contents
Protein chains
344 a.a.
Ligands
CXS ×2
PDB id:
3tw5
Name: Transferase
Title: Crystal structure of the gp42 transglutaminase from phytopht
Structure: Transglutaminase elicitor. Chain: a, b. Fragment: transglutaminase domain. Engineered: yes. Mutation: yes
Source: Phytophthora sojae. Organism_taxid: 67593. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Resolution:
2.95Å     R-factor:   0.216     R-free:   0.234
Authors: K.Reiss,E.Kirchner,G.Zocher,T.Stehle
Key ref: K.Reiss et al. (2011). Structural and phylogenetic analyses of the GP42 transglutaminase from Phytophthora sojae reveal an evolutionary relationship between oomycetes and marine Vibrio bacteria. J Biol Chem, 286, 42585-42593. PubMed id: 21994936 DOI: 10.1074/jbc.M111.290544
Date:
21-Sep-11     Release date:   12-Oct-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6Q475  (Q6Q475_PHYSO) -  Transglutaminase elicitor
Seq:
Struc:
 
Seq:
Struc:
529 a.a.
344 a.a.*
Key:    PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.3.2.13  - Protein-glutamine gamma-glutamyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Protein glutamine
+ alkylamine
= protein N(5)-alkylglutamine
+ NH(3)
      Cofactor: Ca(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M111.290544 J Biol Chem 286:42585-42593 (2011)
PubMed id: 21994936  
 
 
Structural and phylogenetic analyses of the GP42 transglutaminase from Phytophthora sojae reveal an evolutionary relationship between oomycetes and marine Vibrio bacteria.
K.Reiss, E.Kirchner, M.Gijzen, G.Zocher, B.Löffelhardt, T.Nürnberger, T.Stehle, F.Brunner.
 
  ABSTRACT  
 
Transglutaminases (TGases) are ubiquitous enzymes that catalyze selective cross-linking between protein-bound glutamine and lysine residues; the resulting isopeptide bond confers high resistance to proteolysis. Phytophthora sojae, a pathogen of soybean, secretes a Ca(2+)-dependent TGase (GP42) that is activating defense responses in both host and non-host plants. A GP42 fragment of 13 amino acids, termed Pep-13, was shown to be absolutely indispensable for both TGase and elicitor activity. GP42 does not share significant primary sequence similarity with known TGases from mammals or bacteria. This suggests that GP42 has evolved novel structural and catalytic features to support enzymatic activity. We have solved the crystal structure of the catalytically inactive point mutant GP42 (C290S) at 2.95 Å resolution and identified residues involved in catalysis by mutational analysis. The protein comprises three domains that assemble into an elongated structure. Although GP42 has no structural homolog, its core region displays significant similarity to the catalytic core of the Mac-1 cysteine protease from Group A Streptococcus, a member of the papain-like superfamily of cysteine proteases. Proteins that are taxonomically related to GP42 are only present in plant pathogenic oomycetes belonging to the order of the Peronosporales (e.g. Phytophthora, Hyaloperonospora, and Pythium spp.) and in marine Vibrio bacteria. This suggests that a lateral gene transfer event may have occurred between bacteria and oomycetes. Our results offer a basis to design and use highly specific inhibitors of the GP42-like TGase family that may impair the growth of important oomycete and bacterial pathogens.