1ld4
From Proteopedia
(New page: 200px<br /><applet load="1ld4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ld4, resolution 11.4Å" /> '''Placement of the Str...) |
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| - | [[Image:1ld4.gif|left|200px]]<br /><applet load="1ld4" size=" | + | [[Image:1ld4.gif|left|200px]]<br /><applet load="1ld4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ld4, resolution 11.4Å" /> | caption="1ld4, resolution 11.4Å" /> | ||
'''Placement of the Structural Proteins in Sindbis Virus'''<br /> | '''Placement of the Structural Proteins in Sindbis Virus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the lipid-enveloped Sindbis virus has been determined by | + | The structure of the lipid-enveloped Sindbis virus has been determined by fitting atomic resolution crystallographic structures of component proteins into an 11-A resolution cryoelectron microscopy map. The virus has T=4 quasisymmetry elements that are accurately maintained between the external glycoproteins, the transmembrane helical region, and the internal nucleocapsid core. The crystal structure of the E1 glycoprotein was fitted into the cryoelectron microscopy density, in part by using the known carbohydrate positions as restraints. A difference map showed that the E2 glycoprotein was shaped similarly to E1, suggesting a possible common evolutionary origin for these two glycoproteins. The structure shows that the E2 glycoprotein would have to move away from the center of the trimeric spike in order to expose enough viral membrane surface to permit fusion with the cellular membrane during the initial stages of host infection. The well-resolved E1-E2 transmembrane regions form alpha-helical coiled coils that were consistent with T=4 symmetry. The known structure of the capsid protein was fitted into the density corresponding to the nucleocapsid, revising the structure published earlier. |
==About this Structure== | ==About this Structure== | ||
| - | 1LD4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus] with UNX as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LD4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Sindbis_virus Sindbis virus] with <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LD4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Sindbis virus]] | [[Category: Sindbis virus]] | ||
| - | [[Category: Baker, T | + | [[Category: Baker, T S.]] |
| - | [[Category: Kuhn, R | + | [[Category: Kuhn, R J.]] |
[[Category: Mukhopadhyay, S.]] | [[Category: Mukhopadhyay, S.]] | ||
| - | [[Category: Pletnev, S | + | [[Category: Pletnev, S V.]] |
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: Zhang, W.]] | [[Category: Zhang, W.]] | ||
[[Category: UNX]] | [[Category: UNX]] | ||
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[[Category: transmembrane coiled coils]] | [[Category: transmembrane coiled coils]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:48 2008'' |
Revision as of 11:43, 21 February 2008
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Placement of the Structural Proteins in Sindbis Virus
Overview
The structure of the lipid-enveloped Sindbis virus has been determined by fitting atomic resolution crystallographic structures of component proteins into an 11-A resolution cryoelectron microscopy map. The virus has T=4 quasisymmetry elements that are accurately maintained between the external glycoproteins, the transmembrane helical region, and the internal nucleocapsid core. The crystal structure of the E1 glycoprotein was fitted into the cryoelectron microscopy density, in part by using the known carbohydrate positions as restraints. A difference map showed that the E2 glycoprotein was shaped similarly to E1, suggesting a possible common evolutionary origin for these two glycoproteins. The structure shows that the E2 glycoprotein would have to move away from the center of the trimeric spike in order to expose enough viral membrane surface to permit fusion with the cellular membrane during the initial stages of host infection. The well-resolved E1-E2 transmembrane regions form alpha-helical coiled coils that were consistent with T=4 symmetry. The known structure of the capsid protein was fitted into the density corresponding to the nucleocapsid, revising the structure published earlier.
About this Structure
1LD4 is a Protein complex structure of sequences from Saccharomyces cerevisiae and Sindbis virus with as ligand. Full crystallographic information is available from OCA.
Reference
Placement of the structural proteins in Sindbis virus., Zhang W, Mukhopadhyay S, Pletnev SV, Baker TS, Kuhn RJ, Rossmann MG, J Virol. 2002 Nov;76(22):11645-58. PMID:12388725
Page seeded by OCA on Thu Feb 21 13:43:48 2008
Categories: Protein complex | Saccharomyces cerevisiae | Sindbis virus | Baker, T S. | Kuhn, R J. | Mukhopadhyay, S. | Pletnev, S V. | Rossmann, M G. | Zhang, W. | UNX | Alphavirus structure | Cryo-electron microscopy | Glycoprotein organization | Icosahedral virus | Nucleocapsid structure | Transmembrane coiled coils
