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Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3 complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-binding mechanism.

Lu D, Shang G, Zhang H, Yu Q, Cong X, Yuan J, He F, Zhu C, Zhao Y, Yin K, Chen Y, Hu J, Zhang X, Yuan Z, Xu S, Hu W, Cang H, Gu L
Mol Microbiol 92 1092-112 (2014)
Related entries: 4m5e, 4m5f, 4n80, 4n88

Cited: 23 times
EuropePMC logo PMID: 24724564

Abstract

The opportunistic pathogen Pseudomonas aeruginosa uses the type VI secretion system (T6SS) to deliver the muramidase Tse3 into the periplasm of rival bacteria to degrade their peptidoglycan (PG). Concomitantly, P. aeruginosa uses the periplasm-localized immunity protein Tsi3 to prevent potential self-intoxication caused by Tse3, and thus gains an edge over rival bacteria in fierce niche competition. Here, we report the crystal structures of Tse3 and the Tse3-Tsi3 complex. Tse3 contains an annexin repeat-like fold at the N-terminus and a G-type lysozyme fold at the C-terminus. One loop in the N-terminal domain (Loop 12) and one helix (α9) from the C-terminal domain together anchor Tse3 and the Tse3-Tsi3 complex to membrane in a calcium-dependent manner in vitro, and this membrane-binding ability is essential for Tse3's activity. In the C-terminal domain, a Y-shaped groove present on the surface likely serves as the PG binding site. Two calcium-binding motifs are also observed in the groove and these are necessary for Tse3 activity. In the Tse3-Tsi3 structure, three loops of Tsi3 insert into the substrate-binding groove of Tse3, and three calcium ions present at the interface of the complex are indispensable for the formation of the Tse3-Tsi3 complex.

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Reviews citing this publication (7)

  1. Pseudomonas aeruginosa: pathogenesis, virulence factors, antibiotic resistance, interaction with host, technology advances and emerging therapeutics. Qin S, Xiao W, Zhou C, Pu Q, Deng X, Lan L, Liang H, Song X, Wu M. Signal Transduct Target Ther 7 199 (2022)
  2. Ribosomally encoded antibacterial proteins and peptides from Pseudomonas. Ghequire MG, De Mot R. FEMS Microbiol Rev 38 523-568 (2014)
  3. Calcium binding proteins and calcium signaling in prokaryotes. Domínguez DC, Guragain M, Patrauchan M. Cell Calcium 57 151-165 (2015)
  4. Molecular weaponry: diverse effectors delivered by the Type VI secretion system. Alcoforado Diniz J, Liu YC, Coulthurst SJ. Cell Microbiol 17 1742-1751 (2015)
  5. Recent advances in understanding Pseudomonas aeruginosa as a pathogen. Klockgether J, Tümmler B. F1000Res 6 1261 (2017)
  6. Effector⁻Immunity Pairs Provide the T6SS Nanomachine its Offensive and Defensive Capabilities. Yang X, Long M, Shen X. Molecules 23 E1009 (2018)
  7. The Activation Mechanism of the Insulin Receptor: A Structural Perspective. Choi E, Bai XC. Annu Rev Biochem 92 247-272 (2023)

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  1. Structural basis of STING binding with and phosphorylation by TBK1. Zhang C, Shang G, Gui X, Zhang X, Bai XC, Chen ZJ. Nature 567 394-398 (2019)
  2. Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Shang G, Zhang C, Chen ZJ, Bai XC, Zhang X. Nature 567 389-393 (2019)
  3. Activation mechanism of the insulin receptor revealed by cryo-EM structure of the fully liganded receptor-ligand complex. Uchikawa E, Choi E, Shang G, Yu H, Bai XC. Elife 8 e48630 (2019)
  4. Structural basis of the activation of type 1 insulin-like growth factor receptor. Li J, Choi E, Yu H, Bai XC. Nat Commun 10 4567 (2019)
  5. Structure of the calcium-dependent type 2 secretion pseudopilus. López-Castilla A, Thomassin JL, Bardiaux B, Zheng W, Nivaskumar M, Yu X, Nilges M, Egelman EH, Izadi-Pruneyre N, Francetic O. Nat Microbiol 2 1686-1695 (2017)
  6. Structure of the Neisseria Adhesin Complex Protein (ACP) and its role as a novel lysozyme inhibitor. Humbert MV, Awanye AM, Lian LY, Derrick JP, Christodoulides M. PLoS Pathog 13 e1006448 (2017)
  7. The structural basis of the Tle4-Tli4 complex reveals the self-protection mechanism of H2-T6SS in Pseudomonas aeruginosa. Lu D, Zheng Y, Liao N, Wei L, Xu B, Liu X, Liu J. Acta Crystallogr D Biol Crystallogr 70 3233-3243 (2014)
  8. Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. Kuo YC, Chen H, Shang G, Uchikawa E, Tian H, Bai XC, Zhang X. Nat Commun 11 1953 (2020)
  9. Letter Structural analysis of Pseudomonas aeruginosa H3-T6SS immunity proteins. Yang XY, Li ZQ, She Z, Geng Z, Xu JH, Gao ZQ, Dong YH. FEBS Lett 590 2787-2796 (2016)
  10. A disordered region in the EvpP protein from the type VI secretion system of Edwardsiella tarda is essential for EvpC binding. Hu W, Anand G, Sivaraman J, Leung KY, Mok YK. PLoS One 9 e110810 (2014)
  11. Sporulation Activated via σW Protects Bacillus from a Tse1 Peptidoglycan Hydrolase Type VI Secretion System Effector. Pérez-Lorente AI, Molina-Santiago C, de Vicente A, Romero D. Microbiol Spectr e0504522 (2023)
  12. The P. aeruginosa effector Tse5 forms membrane pores disrupting the membrane potential of intoxicated bacteria. González-Magaña A, Altuna J, Queralt-Martín M, Largo E, Velázquez C, Montánchez I, Bernal P, Alcaraz A, Albesa-Jové D. Commun Biol 5 1189 (2022)
  13. Structural and SAXS analysis of Tle5-Tli5 complex reveals a novel inhibition mechanism of H2-T6SS in Pseudomonas aeruginosa. Yang XY, Li ZQ, Gao ZQ, Wang WJ, Geng Z, Xu JH, She Z, Dong YH. Protein Sci 26 2083-2091 (2017)
  14. Structural characterization of the Imm52 family protein TsiT in Pseudomonas aeruginosa. She Z, Geng Z, Xu JH, Li YH, Dong YH. Protein Sci 28 971-975 (2019)
  15. A conserved ion channel function of STING mediates noncanonical autophagy and cell death. Xun J, Zhang Z, Lv B, Lu D, Yang H, Shang G, Tan JX. EMBO Rep 25 544-569 (2024)


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