1ei7: Difference between revisions
New page: left|200px<br /><applet load="1ei7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ei7, resolution 2.45Å" /> '''TMV COAT PROTEIN REF... |
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[[Image:1ei7.jpg|left|200px]]<br /><applet load="1ei7" size=" | [[Image:1ei7.jpg|left|200px]]<br /><applet load="1ei7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ei7, resolution 2.45Å" /> | caption="1ei7, resolution 2.45Å" /> | ||
'''TMV COAT PROTEIN REFINED FROM THE 4-LAYER AGGREGATE'''<br /> | '''TMV COAT PROTEIN REFINED FROM THE 4-LAYER AGGREGATE'''<br /> | ||
==Overview== | ==Overview== | ||
Previous x-ray studies (2.8-A resolution) on crystals of tobacco mosaic | Previous x-ray studies (2.8-A resolution) on crystals of tobacco mosaic virus coat protein grown from solutions containing high salt have characterized the structure of the protein aggregate as a dimer of a bilayered cylindrical disk formed by 34 chemically identical subunits. We have determined the crystal structure of the disk aggregate at 2.4-A resolution using x-ray diffraction from crystals maintained at cryogenic temperatures. Two regions of interest have been extensively refined. First, residues of the low-radius loop region, which were not modeled previously, have been traced completely in our electron density maps. Similar to the structure observed in the virus, the right radial helix in each protomer ends around residue 87, after which the protein chain forms an extended chain that extends to the left radial helix. The left radial helix appears as a long alpha-helix with high temperature factors for the main-chain atoms in the inner portion. The side-chain atoms in this region (residues 90-110) are not visible in the electron density maps and are assumed to be disordered. Second, interactions between subunits in the symmetry-related central A pair have been determined. No direct protein-protein interactions are observed in the major overlap region between these subunits; all interactions are mediated by two layers of ordered solvent molecules. The current structure emphasizes the importance of water in biological macromolecular assemblies. | ||
==About this Structure== | ==About this Structure== | ||
1EI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tobacco_mosaic_virus Tobacco mosaic virus]. Full crystallographic information is available from [http:// | 1EI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tobacco_mosaic_virus Tobacco mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Tobacco mosaic virus]] | [[Category: Tobacco mosaic virus]] | ||
[[Category: Bhyravbhatla, B.]] | [[Category: Bhyravbhatla, B.]] | ||
[[Category: Caspar, D | [[Category: Caspar, D L.]] | ||
[[Category: Watowich, S | [[Category: Watowich, S J.]] | ||
[[Category: disordered loops]] | [[Category: disordered loops]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:01 2008'' | ||
Revision as of 13:28, 21 February 2008
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TMV COAT PROTEIN REFINED FROM THE 4-LAYER AGGREGATE
OverviewOverview
Previous x-ray studies (2.8-A resolution) on crystals of tobacco mosaic virus coat protein grown from solutions containing high salt have characterized the structure of the protein aggregate as a dimer of a bilayered cylindrical disk formed by 34 chemically identical subunits. We have determined the crystal structure of the disk aggregate at 2.4-A resolution using x-ray diffraction from crystals maintained at cryogenic temperatures. Two regions of interest have been extensively refined. First, residues of the low-radius loop region, which were not modeled previously, have been traced completely in our electron density maps. Similar to the structure observed in the virus, the right radial helix in each protomer ends around residue 87, after which the protein chain forms an extended chain that extends to the left radial helix. The left radial helix appears as a long alpha-helix with high temperature factors for the main-chain atoms in the inner portion. The side-chain atoms in this region (residues 90-110) are not visible in the electron density maps and are assumed to be disordered. Second, interactions between subunits in the symmetry-related central A pair have been determined. No direct protein-protein interactions are observed in the major overlap region between these subunits; all interactions are mediated by two layers of ordered solvent molecules. The current structure emphasizes the importance of water in biological macromolecular assemblies.
About this StructureAbout this Structure
1EI7 is a Single protein structure of sequence from Tobacco mosaic virus. Full crystallographic information is available from OCA.
ReferenceReference
Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution., Bhyravbhatla B, Watowich SJ, Caspar DL, Biophys J. 1998 Jan;74(1):604-15. PMID:9449361
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