The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Topologically Linked Protein Rings in the Bacteriophage HK97 Capsid
Abstract
The crystal structure of the double-stranded DNA bacteriophage HK97 mature empty capsid was determined at 3.6 angstrom resolution. The 660 angstrom diameter icosahedral particle contains 420 subunits with a new fold. The final capsid maturation step is an autocatalytic reaction that creates 420 isopeptide bonds between proteins. Each subunit is joined to two of its neighbors by ligation of the side-chain lysine 169 to asparagine 356. This generates 12 pentameric and 60 hexameric rings of covalently joined subunits that loop through each other, creating protein chainmail: topologically linked protein catenanes arranged with icosahedral symmetry. Catenanes have not been previously observed in proteins and provide a stabilization mechanism for the very thin HK97 capsid.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The three-dimensional structure of the bacterial virus MS2
Valegård, K., Liljas, L., Fridborg, K., & Unge, T. (1990) · Nature · doi:10.1038/345036a0 · Cited by 411
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Metadata
- Authors
- Wikoff, W. R., Liljas, L., Duda, R. L., Tsuruta, H., Hendrix, R. W., & Johnson, J. E.
- Venue
- Science
- Published
- 2000-09-22
- Volume
- 289
- Issue
- 5487
- Pages
- 2129-2133
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2131209038
- Cited by
- 729
- References
- 2
- FWCI
- 11.89
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wikoff, W. R., Liljas, L., Duda, R. L., Tsuruta, H., Hendrix, R. W., & Johnson, J. E. (2000). Topologically Linked Protein Rings in the Bacteriophage HK97 Capsid. Science. https://doi.org/10.1126/science.289.5487.2129
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