3TW5

Crystal structure of the GP42 transglutaminase from Phytophthora sojae

Summary for 3TW5

• Entry DOI: 10.2210/pdb3tw5/pdb
• Descriptor: Transglutaminase elicitor, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID (2 entities in total)
• Functional Keywords: cysteine protease, convergent evolution, innate immunity, pathogen-associated molecular pattern (pamp), phytophthora, tranglutaminase, transferase
• Biological source: Phytophthora sojae
• Total number of polymer chains: 2
• Total formula weight: 80891.93

Authors

Reiss, K.,Kirchner, E.,Zocher, G.,Stehle, T. (deposition date: 2011-09-21, release date: 2011-10-12, Last modification date: 2024-10-16)

Primary citation

Reiss, K.,Kirchner, E.,Gijzen, M.,Zocher, G.,Loffelhardt, B.,Nurnberger, T.,Stehle, T.,Brunner, F.
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, 2011

PubMed 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.

PubMed: 21994936
DOI: 10.1074/jbc.M111.290544

Experimental method

X-RAY DIFFRACTION (2.95 Å)