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Crystal Structure of P22 Tailspike Protein: Interdigitated Subunits in a Thermostable Trimer
Abstract
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 system for genetic and biochemical analysis of protein folding. The x-ray structure of a shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom resolution. Each subunit of the homotrimer contains a large parallel β helix. The interdigitation of the polypeptide chains at the carboxyl termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein.
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Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
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Simpson, D. J., Sacher, J. C., & Szymanski, C. M. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.07.006 · Cited by 36
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Hawkins, N. C., Kizziah, J. L., Hatoum-Aslan, A., & Dokland, T. (2022) · Science Advances · doi:10.1126/sciadv.ade0459 · Cited by 25
Metadata
- Authors
- Steinbacher, S., Seckler, R., Miller, S., Steipe, B., Huber, R., & Reinemer, P.
- Venue
- Science
- Published
- 1994-07-15
- Volume
- 265
- Issue
- 5170
- Pages
- 383-386
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1989073611
- Cited by
- 315
- References
- 1
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- closed
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