1ld4

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|PDB= 1ld4 |SIZE=350|CAPTION= <scene name='initialview01'>1ld4</scene>, resolution 11.4&Aring;
|PDB= 1ld4 |SIZE=350|CAPTION= <scene name='initialview01'>1ld4</scene>, resolution 11.4&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=UNX:UNKNOWN ATOM OR ION'>UNX</scene>
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|LIGAND= <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1wyk|1WYK]], [[1ysa|1YSA]], [[1i9w|1I9W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ld4 OCA], [http://www.ebi.ac.uk/pdbsum/1ld4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ld4 RCSB]</span>
}}
}}
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[[Category: Rossmann, M G.]]
[[Category: Rossmann, M G.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
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[[Category: UNX]]
 
[[Category: alphavirus structure]]
[[Category: alphavirus structure]]
[[Category: cryo-electron microscopy]]
[[Category: cryo-electron microscopy]]
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[[Category: transmembrane coiled coil]]
[[Category: transmembrane coiled coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:20 2008''

Revision as of 19:01, 30 March 2008


PDB ID 1ld4

Drag the structure with the mouse to rotate
, resolution 11.4Å
Ligands:
Related: 1WYK, 1YSA, 1I9W


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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