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Atomic‐resolution crystal structure of the antiviral lectin scytovirin
Author(s) -
Moulaei Tinoush,
Botos Istvan,
Ziółkowska Natasza E.,
Bokesch Heidi R.,
Krumpe Lauren R.,
McKee Tawnya C.,
O'Keefe Barry R.,
Dauter Zbigniew,
Wlodawer Alexander
Publication year - 2007
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073157507
Subject(s) - crystallography , resolution (logic) , crystal structure , lectin , chemistry , crystal (programming language) , molecule , sequence (biology) , biochemistry , organic chemistry , artificial intelligence , computer science , programming language
The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single‐wavelength anomalous scattering and refined with data extending to 1.3 Å and 1.0 Å resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 Å for 40 pairs of Cα atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N‐ and C‐terminal domains of 5.3 Å and 3.7 Å, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies.