Share This Author
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.
- S. Steinbacher, R. Seckler, S. Miller, B. Steipe, R. Huber, P. Reinemer
- Biology, ChemistryScience
- 15 July 1994
The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model…
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…
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.
Structure of the Receptor-Binding Protein of Bacteriophage Det7: a Podoviral Tail Spike in a Myovirus
The authors' data suggest receptor-binding module exchange between podoviruses and myovirus in the course of bacteriophage evolution.
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.
- S. Steinbacher, U. Baxa, S. Miller, A. Weintraub, R. Seckler, R. Huber
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 October 1996
Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.
Tailspike Interactions with Lipopolysaccharide Effect DNA Ejection from Phage P22 Particles in Vitro*
- Dorothee Andres, Christine Hanke, U. Baxa, A. Seul, S. Barbirz, R. Seckler
- BiologyThe Journal of Biological Chemistry
- 3 September 2010
Using phage particles reconstituted with purified mutant TSP in vitro, it was found that the endorhamnosidase activity of TSP degrading the O-antigen polysaccharide was required prior to DNA ejection in vitro and DNA replication in vivo.
Crystal structure of Escherichia coli phage HK620 tailspike: podoviral tailspike endoglycosidase modules are evolutionarily related
- S. Barbirz, Jürgen J. Müller, C. Uetrecht, A. Clark, U. Heinemann, R. Seckler
- BiologyMolecular microbiology
- 1 July 2008
It is proposed that the tailspike genes of P22, Sf6 and HK620 have a common precursor and are not mosaics of unrelated gene fragments.
Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state.
Tail morphology controls DNA release in two Salmonella phages with one lipopolysaccharide receptor recognition system
- Dorothee Andres, Y. Roske, C. Doering, U. Heinemann, R. Seckler, S. Barbirz
- BiologyMolecular microbiology
- 1 March 2012
In vitro DNA ejection in long‐tailed siphovirus 9NA and short‐tailed podovirus P22 upon incubation with Salmonella typhimurium lipopolysaccharide (LPS) is analysed and suggests that tail morphology influences the efficiencies of particle opening given an identical initial receptor interaction event.
Mechanism of phage P22 tailspike protein folding mutations
Temperature‐sensitive folding (tsf) and global‐tsf‐suppressor (su) point mutations affect the folding yields of the trimeric, thermostable phage P22 tailspike endorhamnosidase at elevated…
Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine.
- M. Wunderlich, A. Otto, K. Maskos, M. Mücke, R. Seckler, R. Glockshuber
- Biology, ChemistryJournal of molecular biology
- 17 March 1995
The function of the catalytic cysteine residues in DsbA, a PDI-related protein required for disulfide formation in the periplasmic space of Escherichia coli, is investigated by replacing C30 and C33 with alanine and finding that the single active-site thiol group of C30 is sufficient fordisulfide-isomerase activity of the DSBA protein.