About: 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 1 1 Edited by K. Nagai

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About: 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 1 1 Edited by K. Nagai Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	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 1 1 Edited by K. Nagai
Creator	Baxa, Ulrich Huber, Robert Miller, Stefan Seckler, Robert Steinbacher, Stefan »more»
source	Elsevier; Medline; PMC
abstract	Abstract The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-binding domains. We report the crystal structure of the head-binding domain of P22 tailspike protein at 2.3 Å resolution, solved with a recombinant telluromethionine derivative and non-crystallographic symmetry averaging. The trimeric dome-like structure is formed by two perpendicular β-sheets of five and three strands, respectively in each subunit and caps a three-helix bundle observed in the structure of the C-terminal receptor binding and cleaving fragment, reported here after full refinement at 1.56 Å resolution. In the central part of the receptor binding fragment, three parallel β-helices of 13 complete turns are associated side-by-side, while the three polypeptide strands merge into a single domain towards their C termini, with close interdigitation at the junction to the β-helix part. Complex structures with receptor fragments from S. typhimurium, S. enteritidis and S. typhi253Ty determined at 1.8 Å resolution are described in detail. Insertions into the β-helix form the O-antigen binding groove, which also harbours the active site residues Asp392, Asp395 and Glu359. In the intact structure of the tailspike protein, head-binding and receptor-binding parts are probably linked by a flexible hinge whose function may be either to deal with shearing forces on the exposed, 150 Å long tailspikes or to allow them to bend during the infection process.
has issue date	1997-04-11(xsd:dateTime)
bibo:doi	10.1006/jmbi.1997.0922
bibo:pmid	9135118
has license	els-covid
sha1sum (hex)	56bd4bd786dd96bfda9f2c096eeed6eee4280ee8
schema:url	https://doi.org/10.1006/jmbi.1997.0922
resource representing a document's title	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 1 1 Edited by K. Nagai
has PubMed Central identifier	PMC7172399
has PubMed identifier	9135118
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:56bd4bd786dd96bfda9f2c096eeed6eee4280ee8#body_text
is schema:about of	named entity 'receptor' named entity 'residues' named entity 'assembly' named entity 'complete' named entity 'recognises' »more»

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