Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage

Steinbacher, Stefan; Miller, Stefan; Baxa, Ulrich; Budiša, Nediljko; Weintraub, Andrej; Seckler, Robert; Huber, Robert

doi:10.1006/jmbi.1997.0922

Cited by 170 publications

(206 citation statements)

References 60 publications

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“…However, aside from their globular shape, the C-terminal extensions share no further structural similarity with the reported CIMCDs. The parallel-β-helix tailspike proteins (TSP) of the Podoviridae bacteriophages P22, Phi29, HK620, and Sf6 all contain a C-terminal trimerization domain that predominantly consists of β-strands, unlike the CIMCDs, which are mainly α-helical [19][20][21][22][23] . In the extensively studied P22 TSP, a combination of a triple β-helix, a β-prism and an antiparallel β-sheet interact in order to form a trimerization domain 21,22 .…”

Section: Discussionmentioning

confidence: 99%

“…The parallel-β-helix tailspike proteins (TSP) of the Podoviridae bacteriophages P22, Phi29, HK620, and Sf6 all contain a C-terminal trimerization domain that predominantly consists of β-strands, unlike the CIMCDs, which are mainly α-helical [19][20][21][22][23] . In the extensively studied P22 TSP, a combination of a triple β-helix, a β-prism and an antiparallel β-sheet interact in order to form a trimerization domain 21,22 . In the recently described neck appendages of bacteriophage Phi29, a C-terminal extension, which mainly consists of two β-barrels, aids maturation of the parallel-β-helix pre-protein in an ATP-driven reaction 23 .…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Crystal structure of an intramolecular chaperone mediating triple–β-helix folding

Schulz

Dickmanns

Urlaub

et al. 2010

Nat Struct Mol Biol

106

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Proteins fold into their functional three-dimensional structure based on the information encoded in the residue sequence 1 . In all domains of life, various strategies evolved to assist folding processes in order to prevent immediate misfolding and aggregation of the nascent polypeptide chain. In the crowded cellular environment, protein folding is often aided by molecular chaperones. Molecular chaperones differ in size, function and energy dependence; however, all have in common to bind to the unfolded state of the protein in order to facilitate or mediate assembly of the correct three-dimensional structure 2,3 . In contrast to molecular chaperones, the intramolecular chaperones (IMCs) constitute a different class of chaperones. As part of the polypeptide chain, the IMC is typically cleaved off the target protein after the folding process is completed. Two classes of IMCs can be distinguished: class I IMCs assist the protein to fold into the correct tertiary structure, whereas class II IMCs are involved in quaternary structure assembly 4 . In contrast to many molecular chaperones, no evidence for an ATP-driven cleavage reaction could be found in IMCs. An example of a class II intramolecular chaperone has been identified in viral tailspike and fiber proteins. These proteins are functionally unrelated but share a highly conserved chaperone domain at their C terminus (C-terminal intramolecular chaperone domain, CIMCD), which is cleaved at a conserved position in an autoproteolytic reaction 5 . It was shown that the covalent linkage between the CIMCD and N-terminal pre-protein is necessary for correct folding, indicating that an in trans function of the chaperone is impossible 5 . Furthermore, it could be shown that some of the chaperone domains are exchangeable between the different preproteins 5,6 . While the three-dimensional structures of the CIMCDs are as yet unknown, the crystal structure of N-terminally truncated mature endoNF shows that the homotrimeric enzyme comprises a triple β-helix involved in substrate recognition 7 . This triple β-helix and the related triple-β-spiral motif have been identified in various proteins, which often play a role as virulence factors 8 . In triple β-helices, three polypeptide chains wind around a common threefold symmetry axis, conferring an extraordinary stability to the protein. The rigid elongated shape allows triple β-helix-comprising proteins to protrude from a pathogen's surface in order to interact with flexible host cell receptors, like lipopolysaccharides 9 . However, proper assembly of triple-β-helical folds poses to be difficult in the absence of a trimerization domain 10 . Hence, most triple β-helices depend on a C-terminal extension for trimerization and correct assembly 11 .Here we present the crystal structures of two representatives of a large group of systematically, functionally and structurally similar intramolecular chaperones: the Escherichia coli phage K1F endosilidase CIMCD and the Bacillus subtilis phage GA-1 neck appendage protein CIMCD. Furthermore...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Crystal structure of an intramolecular chaperone mediating triple–β-helix folding

Schulz

Dickmanns

Urlaub

et al. 2010

Nat Struct Mol Biol

106

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“…The structure of the P22 trimeric TSP has been described in detail in x-ray crystallographic and cryoelectron microscopy studies, Figure 1 (Pymol representation of xray coordinates) [6][7][8][9][10][11]. The P22 TSP consists of three structural elements: 1) The P22 TSP N-terminal domain (P22 TSP NTD), containing the first 108 amino acids (aa1-aa108) from each of three TSPs, exists as a domelike structure, Figure 2 [9]. The P22 TSP NTD is necessary for P22 phage particle assembly [12].…”

Section: The Structural Domains Of the P22 Tailspike Proteinmentioning

confidence: 99%

Stem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein

Palmer¹,

Williams²,

Dean³

et al. 2013

AJMR

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The P22 tailspike protein is an intensely studied protein whose structure and sequence has been described. However, a study, describing important protein interactions related to its function at the N-terminal domain, has been lacking. The P22 tailspike protein (TSP) consists of three identical polypeptide chains of 666aa. The first 108 of the 666aa in the P22 TSP form a trimeric N-terminal domain (NTD). Each of the three chains of the trimeric NTD contributes to the formation of a dome-like structure. Our studies suggest that a short stretch of amino acids located within the first fifteen amino acids of the P22 TSP NTD is critical for the stability of the dome structure formed by the first 108aa of the P22 TSP NTD. The first 23aa are located within this dome-like structure and have been dubbed the "stem" of the NTD. Although amino acid residues in the first 15aa (lower stem) are critical, deletion analysis and in vitro assembly studies implicate the rest of the stem in additional stabilizing interactions. Our studies implicate a common protein-protein interaction motif made up of interchain hydrophobic contacts between adjacent chains

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“…Its carboxy terminus is responsible for the hydrolysis of the oligosaccharide receptor at the outer cell membrane [1], allowing the phage particles to positionate for DNA injection, while the amino terminal domain connects the TSP to the phage neck [2]. The native TSP is unusually resistant to proteolysis and to temperature-and detergent-mediated denaturation, whereas the folding intermediates are extremely thermolabile [3].…”

Section: Introductionmentioning

confidence: 99%

Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N‐terminal fusion mutant

Carbonell

Villaverde

1998

FEBS Letters

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The tailspike protein (TSP) of bacteriophage P22 is a homotrimeric multifunctional protein responsible for cell attachment and hydrolysis of the Salmonella typhimurium host cell receptor. Despite the folding of TSP involves the formation of thermolabile intermediates, the mature protein is extremely resistant to heat and detergent denaturation. We have analyzed the thermal resistance and unfolding pathway of two mutant, functional TSPs carrying end-terminal peptide fusions. Whereas the C-terminal fusion has minor effects on the TSP stability, the presence of a 23-mer foreign peptide at the N terminus (protein ATSP) results in a significant enhancement of the thermal resistance by retarding the first transition step of the unfolding process. At 65³C and in 2% SDS, the unfolding rate constant for the transition from the native to the unfolding intermediate is 9.3U10 3R s 3I for ATSP versus 1.7U10 3Q s 3I for wild-type TSP. On the other hand, the electrophoretic mobility of ATSP intermediates is greatly affected, proving structural modifications induced by the fused peptide. These results suggest a critical participation of the N-terminal domain in the unfolding kinetic barriers generated during the TSP denaturation pathway.z 1998 Federation of European Biochemical Societies.

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Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage

Cited by 170 publications

References 60 publications

Crystal structure of an intramolecular chaperone mediating triple–β-helix folding

Crystal structure of an intramolecular chaperone mediating triple–β-helix folding

Stem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein

Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N‐terminal fusion mutant

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