BIOMAT Database Logo BIOMAT Database Logo

Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. 1996

S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, Germany.

The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011135 Polysaccharides, Bacterial Polysaccharides found in bacteria and in capsules thereof. Bacterial Polysaccharides
D011991 Receptors, Virus Specific molecular components of the cell capable of recognizing and interacting with a virus, and which, after binding it, are capable of generating some signal that initiates the chain of events leading to the biological response. Viral Entry Receptor,Viral Entry Receptors,Virus Attachment Factor,Virus Attachment Factors,Virus Attachment Receptor,Virus Attachment Receptors,Virus Entry Receptor,Virus Entry Receptors,Virus Receptor,Virus Receptors,Attachment Factor, Virus,Attachment Factors, Virus,Attachment Receptor, Virus,Attachment Receptors, Virus,Entry Receptor, Viral,Entry Receptor, Virus,Entry Receptors, Viral,Entry Receptors, Virus,Receptor, Viral Entry,Receptor, Virus,Receptor, Virus Attachment,Receptor, Virus Entry,Receptors, Viral Entry,Receptors, Virus Attachment,Receptors, Virus Entry
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D006026 Glycoside Hydrolases Any member of the class of enzymes that catalyze the cleavage of the glycosidic linkage of glycosides and the addition of water to the resulting molecules. Endoglycosidase,Exoglycosidase,Glycohydrolase,Glycosidase,Glycosidases,Glycoside Hydrolase,Endoglycosidases,Exoglycosidases,Glycohydrolases,Hydrolase, Glycoside,Hydrolases, Glycoside
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D012475 Salmonella A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that utilizes citrate as a sole carbon source. It is pathogenic for humans, causing enteric fevers, gastroenteritis, and bacteremia. Food poisoning is the most common clinical manifestation. Organisms within this genus are separated on the basis of antigenic characteristics, sugar fermentation patterns, and bacteriophage susceptibility.
D017100 Bacteriophage P22 A species of temperate bacteriophage in the genus P22-like viruses, family PODOVIRIDAE, that infects SALMONELLA species. The genome consists of double-stranded DNA, terminally redundant, and circularly permuted. Enterobacteria phage P22,P22 Phage,Phage P22,P22 Phages,Phage, P22,Phages, P22
D017376 Viral Tail Proteins Proteins found in the tail sections of DNA and RNA viruses. It is believed that these proteins play a role in directing chain folding and assembly of polypeptide chains. Virus Tail Proteins,Proteins, Viral Tail,Proteins, Virus Tail,Tail Proteins, Viral,Tail Proteins, Virus

Related Publications

S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Interaction of a Salmonella enteritidis O-antigen octasaccharide with the phage P22 tailspike protein by NMR spectroscopy and docking studies.
February 2008, Glycoconjugate journal,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Mechanism of phage P22 tailspike protein folding mutations.
November 1993, Protein science : a publication of the Protein Society,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
In vitro folding pathway of phage P22 tailspike protein.
July 1991, Biochemistry,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.
January 2003, The Journal of biological chemistry,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
July 1994, Science (New York, N.Y.),
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Folding and function of repetitive structure in the homotrimeric phage P22 tailspike protein.
January 1998, Journal of structural biology,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
An essential serotype recognition pocket on phage P22 tailspike protein forces Salmonella enterica serovar Paratyphi A O-antigen fragments to bind as nonsolution conformers.
April 2013, Glycobiology,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Carbohydrate binding of Salmonella phage P22 tailspike protein and its role during host cell infection.
October 2010, Biochemical Society transactions,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro.
February 1993, The Journal of biological chemistry,
S Steinbacher, and U Baxa, and S Miller, and A Weintraub, and R Seckler, and R Huber
Self-Competitive Inhibition of the Bacteriophage P22 Tailspike Endorhamnosidase by O-Antigen Oligosaccharides.
December 2020, Biochemistry,
Copied contents to your clipboard!