1m3y

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(New page: 200px<br /><applet load="1m3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3y, resolution 2.0&Aring;" /> '''The Structure of Majo...)
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'''The Structure of Major Capsid protein of a large, lipid containing, DNA virus'''<br />
'''The Structure of Major Capsid protein of a large, lipid containing, DNA virus'''<br />
==Overview==
==Overview==
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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.
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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==
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1M3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with NDG, MAN, NAG and HG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M3Y OCA].
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1M3Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=MAN:'>MAN</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=HG:'>HG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3Y OCA].
==Reference==
==Reference==
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[[Category: Paramecium bursaria chlorella virus 1]]
[[Category: Paramecium bursaria chlorella virus 1]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baker, T.S.]]
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[[Category: Baker, T S.]]
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[[Category: Etten, J.L.Van.]]
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[[Category: Etten, J L.Van.]]
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[[Category: Graves, M.V.]]
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[[Category: Graves, M V.]]
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[[Category: Gurnon, J.R.]]
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[[Category: Gurnon, J R.]]
[[Category: Nandhagopal, N.]]
[[Category: Nandhagopal, N.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
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[[Category: Simpson, A.A.]]
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[[Category: Simpson, A A.]]
[[Category: Yan, X.]]
[[Category: Yan, X.]]
[[Category: HG]]
[[Category: HG]]
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[[Category: pbcv-1]]
[[Category: pbcv-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:13 2008''

Revision as of 11:51, 21 February 2008


1m3y, resolution 2.0Å

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The Structure of Major Capsid protein of a large, lipid containing, DNA virus

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

1M3Y is a Single protein structure of sequence from Paramecium bursaria chlorella virus 1 with , , and as ligands. 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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