2qt4

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==Overview==
==Overview==
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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 A and 1.0 A 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 A for 40 pairs of Calpha 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 A and 3.7 A, 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.
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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 A and 1.0 A 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 A for 40 pairs of Calpha 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 A and 3.7 A, 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.
==About this Structure==
==About this Structure==
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[[Category: Moulaei, T.]]
[[Category: Moulaei, T.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
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[[Category: Ziolkowska, N.E.]]
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[[Category: Ziolkowska, N E.]]
[[Category: lectin]]
[[Category: lectin]]
[[Category: sugar binding protein]]
[[Category: sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:59:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:42:02 2008''

Revision as of 16:42, 21 February 2008


2qt4, resolution 1.300Å

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Atomic-resolution crystal structure of the natural form of Scytovirin

Overview

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 A and 1.0 A 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 A for 40 pairs of Calpha 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 A and 3.7 A, 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.

About this Structure

2QT4 is a Protein complex structure of sequences from Scytonema varium. Full crystallographic information is available from OCA.

Reference

Atomic-resolution crystal structure of the antiviral lectin scytovirin., Moulaei T, Botos I, Ziolkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A, Protein Sci. 2007 Dec;16(12):2756-60. Epub 2007 Oct 26. PMID:17965185

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