1m4x
From Proteopedia
(New page: 200px<br /><applet load="1m4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4x" /> '''PBCV-1 virus capsid, quasi-atomic model'''<b...) |
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| - | [[Image:1m4x.gif|left|200px]]<br /><applet load="1m4x" size=" | + | [[Image:1m4x.gif|left|200px]]<br /><applet load="1m4x" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''PBCV-1 virus capsid, quasi-atomic model'''<br /> | '''PBCV-1 virus capsid, quasi-atomic model'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Paramecium bursaria Chlorella virus type 1 (PBCV-1) is a very large, icosahedral virus containing an internal membrane enclosed within a | + | Paramecium bursaria Chlorella virus type 1 (PBCV-1) is a very large, icosahedral virus containing an internal membrane enclosed within a glycoprotein coat consisting of pseudohexagonal arrays of trimeric capsomers. Each capsomer is composed of three molecules of the major capsid protein, Vp54, the 2.0-A resolution structure of which is reported here. Four N-linked and two O-linked glycosylation sites were identified. The N-linked sites are associated with nonstandard amino acid motifs as a result of glycosylation by virus-encoded enzymes. Each monomer of the trimeric structure consists of two eight-stranded, antiparallel beta-barrel, "jelly-roll" domains related by a pseudo-sixfold rotation. The fold of the monomer and the pseudo-sixfold symmetry of the capsomer resembles that of the major coat proteins in the double-stranded DNA bacteriophage PRD1 and the double-stranded DNA human adenoviruses, as well as the viral proteins VP2-VP3 of picornaviruses. The structural similarities among these diverse groups of viruses, whose hosts include bacteria, unicellular eukaryotes, plants, and mammals, make it probable that their capsid proteins have evolved from a common ancestor that had already acquired a pseudo-sixfold organization. The trimeric capsid protein structure was used to produce a quasi-atomic model of the 1,900-A diameter PBCV-1 outer shell, based on fitting of the Vp54 crystal structure into a three-dimensional cryoelectron microscopy image reconstruction of the virus. |
==About this Structure== | ==About this Structure== | ||
| - | 1M4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_type_1_(pbcv-1) Paramecium bursaria chlorella virus type 1 (pbcv-1)]. Full crystallographic information is available from [http:// | + | 1M4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_type_1_(pbcv-1) Paramecium bursaria chlorella virus type 1 (pbcv-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Paramecium bursaria chlorella virus type 1 (pbcv-1)]] | [[Category: Paramecium bursaria chlorella virus type 1 (pbcv-1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, T | + | [[Category: Baker, T S.]] |
| - | [[Category: Etten, J | + | [[Category: Etten, J L.Van.]] |
| - | [[Category: Graves, M | + | [[Category: Graves, M V.]] |
| - | [[Category: Gurnon, J | + | [[Category: Gurnon, J R.]] |
[[Category: Nandhagopal, N.]] | [[Category: Nandhagopal, N.]] | ||
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
| - | [[Category: Simpson, A | + | [[Category: Simpson, A A.]] |
[[Category: Yan, X.]] | [[Category: Yan, X.]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
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[[Category: icosahedral virus capsid]] | [[Category: icosahedral virus capsid]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:36 2008'' |
Revision as of 11:51, 21 February 2008
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PBCV-1 virus capsid, quasi-atomic model
Overview
Paramecium bursaria Chlorella virus type 1 (PBCV-1) is a very large, icosahedral virus containing an internal membrane enclosed within a glycoprotein coat consisting of pseudohexagonal arrays of trimeric capsomers. Each capsomer is composed of three molecules of the major capsid protein, Vp54, the 2.0-A resolution structure of which is reported here. Four N-linked and two O-linked glycosylation sites were identified. The N-linked sites are associated with nonstandard amino acid motifs as a result of glycosylation by virus-encoded enzymes. Each monomer of the trimeric structure consists of two eight-stranded, antiparallel beta-barrel, "jelly-roll" domains related by a pseudo-sixfold rotation. The fold of the monomer and the pseudo-sixfold symmetry of the capsomer resembles that of the major coat proteins in the double-stranded DNA bacteriophage PRD1 and the double-stranded DNA human adenoviruses, as well as the viral proteins VP2-VP3 of picornaviruses. The structural similarities among these diverse groups of viruses, whose hosts include bacteria, unicellular eukaryotes, plants, and mammals, make it probable that their capsid proteins have evolved from a common ancestor that had already acquired a pseudo-sixfold organization. The trimeric capsid protein structure was used to produce a quasi-atomic model of the 1,900-A diameter PBCV-1 outer shell, based on fitting of the Vp54 crystal structure into a three-dimensional cryoelectron microscopy image reconstruction of the virus.
About this Structure
1M4X is a Single protein structure of sequence from Paramecium bursaria chlorella virus type 1 (pbcv-1). Full crystallographic information is available from OCA.
Reference
The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus., Nandhagopal N, Simpson AA, Gurnon JR, Yan X, Baker TS, Graves MV, Van Etten JL, Rossmann MG, Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14758-63. Epub 2002 Oct 31. PMID:12411581
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