3ezm
From Proteopedia
(New page: 200px<br /> <applet load="3ezm" size="450" color="white" frame="true" align="right" spinBox="true" caption="3ezm, resolution 1.5Å" /> '''CYANOVIRIN-N'''<br /...) |
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| - | [[Image:3ezm.gif|left|200px]]<br /> | + | [[Image:3ezm.gif|left|200px]]<br /><applet load="3ezm" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="3ezm" size=" | + | |
caption="3ezm, resolution 1.5Å" /> | caption="3ezm, resolution 1.5Å" /> | ||
'''CYANOVIRIN-N'''<br /> | '''CYANOVIRIN-N'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of cyanovirin-N (CV-N), a protein with potent | + | The crystal structure of cyanovirin-N (CV-N), a protein with potent antiviral activity, was solved at 1.5 A resolution by molecular replacement using as the search model the solution structure previously determined by NMR. The crystals belong to the space group P3221 with one monomer of CV-N in each asymmetric unit. The primary structure of CV-N contains 101 residues organized in two domains, A (residues 1 to 50) and B (residues 51 to 101), with a high degree of internal sequence and structural similarity. We found that under the conditions of the crystallographic experiments (low pH and 26 % isopropanol), two symmetrically related monomers form a dimer by domain swapping, such that domain A of one monomer interacts with domain B' of its crystallographic symmetry mate and vice versa. Because the two swapped domains are distant from each other, domain swapping does not result in additional intramolecular interactions. Even though one of the protein sample solutions that was used for crystallization clearly contained 100 % monomeric CV-N molecules, as judged by various methods, we were only able to obtain crystals containing domain-swapped dimers. With the exception of the unexpected phenomenon of domain swapping, the crystal structure of CV-N is very similar to the NMR structure, with a root-mean-square deviation of 0.55 A for the main-chain atoms, the best agreement reported to date for structures solved using both techniques. |
==About this Structure== | ==About this Structure== | ||
| - | 3EZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http:// | + | 3EZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nostoc_ellipsosporum Nostoc ellipsosporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EZM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hiv-inactivating]] | [[Category: hiv-inactivating]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:30 2008'' |
Revision as of 17:09, 21 February 2008
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CYANOVIRIN-N
Overview
The crystal structure of cyanovirin-N (CV-N), a protein with potent antiviral activity, was solved at 1.5 A resolution by molecular replacement using as the search model the solution structure previously determined by NMR. The crystals belong to the space group P3221 with one monomer of CV-N in each asymmetric unit. The primary structure of CV-N contains 101 residues organized in two domains, A (residues 1 to 50) and B (residues 51 to 101), with a high degree of internal sequence and structural similarity. We found that under the conditions of the crystallographic experiments (low pH and 26 % isopropanol), two symmetrically related monomers form a dimer by domain swapping, such that domain A of one monomer interacts with domain B' of its crystallographic symmetry mate and vice versa. Because the two swapped domains are distant from each other, domain swapping does not result in additional intramolecular interactions. Even though one of the protein sample solutions that was used for crystallization clearly contained 100 % monomeric CV-N molecules, as judged by various methods, we were only able to obtain crystals containing domain-swapped dimers. With the exception of the unexpected phenomenon of domain swapping, the crystal structure of CV-N is very similar to the NMR structure, with a root-mean-square deviation of 0.55 A for the main-chain atoms, the best agreement reported to date for structures solved using both techniques.
About this Structure
3EZM is a Single protein structure of sequence from Nostoc ellipsosporum. Full crystallographic information is available from OCA.
Reference
Crystal structure of cyanovirin-N, a potent HIV-inactivating protein, shows unexpected domain swapping., Yang F, Bewley CA, Louis JM, Gustafson KR, Boyd MR, Gronenborn AM, Clore GM, Wlodawer A, J Mol Biol. 1999 May 7;288(3):403-12. PMID:10329150
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