1no7
From Proteopedia
(New page: 200px<br /><applet load="1no7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1no7, resolution 2.90Å" /> '''Structure of the Lar...) |
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| - | [[Image:1no7.jpg|left|200px]]<br /><applet load="1no7" size=" | + | [[Image:1no7.jpg|left|200px]]<br /><applet load="1no7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1no7, resolution 2.90Å" /> | caption="1no7, resolution 2.90Å" /> | ||
'''Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1'''<br /> | '''Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped | + | Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 A crystal structure of this fragment and its modeling into an 8.5 A resolution electron cryomicroscopy map of the HSV-1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation. |
==About this Structure== | ==About this Structure== | ||
| - | 1NO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | + | 1NO7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, M | + | [[Category: Baker, M L.]] |
| - | [[Category: Bowman, B | + | [[Category: Bowman, B R.]] |
[[Category: Chiu, W.]] | [[Category: Chiu, W.]] | ||
| - | [[Category: Quiocho, F | + | [[Category: Quiocho, F A.]] |
| - | [[Category: Rixon, F | + | [[Category: Rixon, F J.]] |
[[Category: alpha plus beta]] | [[Category: alpha plus beta]] | ||
[[Category: folding nucleus]] | [[Category: folding nucleus]] | ||
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[[Category: viral capsid protein]] | [[Category: viral capsid protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:14 2008'' |
Revision as of 12:08, 21 February 2008
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Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1
Overview
Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 A crystal structure of this fragment and its modeling into an 8.5 A resolution electron cryomicroscopy map of the HSV-1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation.
About this Structure
1NO7 is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
Structure of the herpesvirus major capsid protein., Bowman BR, Baker ML, Rixon FJ, Chiu W, Quiocho FA, EMBO J. 2003 Feb 17;22(4):757-65. PMID:12574112
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