The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins

Webber, Tawnya; Gurung, Sarsati; Saul, Justin M.; Baker, Trenton L.; Spatara, Michelle L.; Freyer, Matthew W.; Robinson, Anne S.; Gage, Matthew J.

doi:10.1042/bj20081449

Cited by 7 publications

(4 citation statements)

References 25 publications

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“…Very recently, the trimerization ability of the isolated carboxyl-terminal domain of P22 tailspike was demonstrated in a fusion chimera with the monomeric maltose binding protein 46. The carboxyl-terminal domain can be visually separated into the β-prism and caudal fin subdomains, although their trimeric structure is stabilizied by the continuous central hydrophobic core 45.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

Boudko

Sasaki

Engel

et al. 2009

Journal of Molecular Biology

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Collagens contain a unique triple helical structure with a repeating sequence -G-X-Y-, where proline and hydroxyproline are major constituents in X and Y positions, respectively. Folding of the collagen triple helix requires trimerization domains. Once trimerized, collagen chains are correctly aligned and the folding of the triple helix proceeds in a zipper-like fashion. Here we report the isolation, characterization and crystal structure of the trimerization domain of human type XVIII collagen, a member of the multiplexin family. This domain differs from all other known trimerization domains in other collagens and exhibits a high trimerization potential at picomolar concentrations. Strong chain association and high specificity of binding are needed for multiplexins, which are present at very low levels.

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Section: Resultsmentioning

confidence: 99%

Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

Boudko

Sasaki

Engel

et al. 2009

Journal of Molecular Biology

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“…The C-terminal domain of TSPs has long been believed as a crucial factor in the trimer formation of the proteins ( 30 , 34 , 45 , 46 ). However, unlike several other TSPs that contain interdigitated or swapped elements following the central β-helix domain, the K2-2 structure described here shows a very limited buried surface in the C-terminal domain, which results in a negative free energy of dissociation (Δ G diss ) when analyzed by PDBePISA.…”

Section: Resultsmentioning

confidence: 99%

Klebsiella pneumoniae K2 capsular polysaccharide degradation by a bacteriophage depolymerase does not require trimer formation

Ye,

Fung,

Lee

et al. 2024

mBio

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Generating fragments of capsular polysaccharides from pathogenic bacteria with crucial antigenic determinants for vaccine development continues to pose challenges. The significance of the C-terminal region of phage tailspike protein (TSP) in relation to its folding and trimer formation remains largely unexplored. The polysaccharide depolymerase described here demonstrates the ability to depolymerize the K2 CPS of K. pneumoniae into tetrasaccharide fragments while retaining the vital O -acetylation modification crucial for immunogenicity. By carefully characterizing the enzyme, elucidating its three-dimensional structures, conducting site-directed mutagenesis, and assessing the antimicrobial efficacy of the mutant enzymes against K2 K. pneumoniae , we offer valuable insights into the mechanism by which this enzyme recognizes and depolymerizes the K2 CPS. Our findings, particularly the discovery that trimer formation is not required for depolymerizing activity, challenge the current understanding of trimer-dependent TSP activity and highlight the catalytic mechanism of the TSP with an intersubunit catalytic center.

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“…Unlike Ø29 and K1F, the P22 C-terminal domain is not cleaved after native trimer folding. However, the isolated C-terminal domain (residues 537–666) of P22 tailspike can function as an independent oligomerization domain 35 . When three maltose binding protein were tethered to a trimeric P22 tailspike C-terminal domain, the chimera chains assembled into a P22 tailspike-like trimer.…”

Section: Introductionmentioning

confidence: 99%

“…However, the isolated C-terminal domain (residues 537–666) of P22 tailspike can function as an independent oligomerization domain. 35 When three maltose binding protein were tethered to a trimeric P22 tailspike C-terminal domain, the chimera chains assembled into a P22 tailspike-like trimer. This suggests a type II IMC function is exhibited by the C-terminal domain of P22 tailspike.…”

Section: Introductionmentioning

confidence: 99%

The C-terminal cysteine annulus participates in auto-chaperone function forSalmonellaphage P22 tailspike folding and assembly

Takata¹,

Haase-Pettingell

King³

2012

Bacteriophage

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Elongated trimeric adhesins are a distinct class of proteins employed by phages and viruses to recognize and bind to their host cells, and by bacteria to bind to their target cells and tissues. The tailspikes of E. coli phage K1F and Bacillus phage Ø29 exhibit auto-chaperone activity in their trimeric C-terminal domains. The P22 tailspike is structurally homologous to those adhesins. Though there are no disulfide bonds or reactive cysteines in the native P22 tailspikes, a set of C-terminal cysteines are very reactive in partially folded intermediates, implying an unusual local conformation in the domain. This is likely to be involved in the auto-chaperone function. We examined the unusual reactivity of C-terminal tailspike cysteines during folding and assembly as a potential reporter of auto-chaperone function. Reaction with IAA blocked productive refolding in vitro, but not off-pathway aggregation. Two-dimensional PAGE revealed that the predominant intermediate exhibiting reactive cysteine side chains was a partially folded monomer. Treatment with reducing reagent promoted native trimer formation from these species, consistent with transient disulfide bonds in the auto-chaperone domain. Limited enzymatic digestion and mass spectrometry of folding and assembly intermediates indicated that the C-terminal domain was compact in the protrimer species. These results indicate that the C-terminal domain of the P22 tailspike folds itself and associates prior to formation of the protrimer intermediate, and not after, as previously proposed. The C-terminal cysteines and triple β-helix domains apparently provide the staging for the correct auto-chaperone domain formation, needed for alignment of P22 tailspike native trimer.

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The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins

Cited by 7 publications

References 25 publications

Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

Crystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization Fold

Klebsiella pneumoniae K2 capsular polysaccharide degradation by a bacteriophage depolymerase does not require trimer formation

The C-terminal cysteine annulus participates in auto-chaperone function forSalmonellaphage P22 tailspike folding and assembly

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