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1p58
From Proteopedia
(New page: 200px<br /><applet load="1p58" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p58" /> '''Complex Organization of Dengue Virus Membran...) |
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| - | [[Image:1p58.gif|left|200px]]<br /><applet load="1p58" size=" | + | [[Image:1p58.gif|left|200px]]<br /><applet load="1p58" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p58" /> | caption="1p58" /> | ||
'''Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction'''<br /> | '''Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Improved technology for reconstructing cryo-electron microscopy (cryo-EM) | + | Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 A by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope (E) and 180 membrane (M) proteins in the lipid envelope. The alpha-helical 'stem' regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The 'anchor' regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus. |
==About this Structure== | ==About this Structure== | ||
| - | 1P58 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http:// | + | 1P58 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P58 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dengue virus type 3]] | [[Category: Dengue virus type 3]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Baker, T | + | [[Category: Baker, T S.]] |
| - | [[Category: Chipman, P | + | [[Category: Chipman, P R.]] |
[[Category: Corver, J.]] | [[Category: Corver, J.]] | ||
| - | [[Category: Johnson, P | + | [[Category: Johnson, P R.]] |
| - | [[Category: Kuhn, R | + | [[Category: Kuhn, R J.]] |
[[Category: Mukhopadhyay, S.]] | [[Category: Mukhopadhyay, S.]] | ||
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
| - | [[Category: Strauss, J | + | [[Category: Strauss, J H.]] |
[[Category: Zhang, W.]] | [[Category: Zhang, W.]] | ||
[[Category: Zhang, Y.]] | [[Category: Zhang, Y.]] | ||
| Line 31: | Line 31: | ||
[[Category: membrane protein m]] | [[Category: membrane protein m]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:14 2008'' |
Revision as of 12:25, 21 February 2008
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Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction
Overview
Improved technology for reconstructing cryo-electron microscopy (cryo-EM) images has now made it possible to determine secondary structural features of membrane proteins in enveloped viruses. The structure of mature dengue virus particles was determined to a resolution of 9.5 A by cryo-EM and image reconstruction techniques, establishing the secondary structural disposition of the 180 envelope (E) and 180 membrane (M) proteins in the lipid envelope. The alpha-helical 'stem' regions of the E molecules, as well as part of the N-terminal section of the M proteins, are buried in the outer leaflet of the viral membrane. The 'anchor' regions of E and the M proteins each form antiparallel E-E and M-M transmembrane alpha-helices, leaving their C termini on the exterior of the viral membrane, consistent with the predicted topology of the unprocessed polyprotein. This is one of only a few determinations of the disposition of transmembrane proteins in situ and shows that the nucleocapsid core and envelope proteins do not have a direct interaction in the mature virus.
About this Structure
1P58 is a Protein complex structure of sequences from Dengue virus type 3. Full crystallographic information is available from OCA.
Reference
Visualization of membrane protein domains by cryo-electron microscopy of dengue virus., Zhang W, Chipman PR, Corver J, Johnson PR, Zhang Y, Mukhopadhyay S, Baker TS, Strauss JH, Rossmann MG, Kuhn RJ, Nat Struct Biol. 2003 Nov;10(11):907-12. Epub 2003 Oct 5. PMID:14528291
Page seeded by OCA on Thu Feb 21 14:25:14 2008
Categories: Dengue virus type 3 | Protein complex | Baker, T S. | Chipman, P R. | Corver, J. | Johnson, P R. | Kuhn, R J. | Mukhopadhyay, S. | Rossmann, M G. | Strauss, J H. | Zhang, W. | Zhang, Y. | Cryo-em | Dengue virus | Flaviviridae | Flavivirus | Glycoprotein e from tick-borne encephalitis virus | Icosahedral virus | Membrane protein m
