1qhd

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(New page: 200px<br /><applet load="1qhd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qhd, resolution 1.95&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qhd.jpg|left|200px]]<br /><applet load="1qhd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qhd, resolution 1.95&Aring;" />
caption="1qhd, resolution 1.95&Aring;" />
'''CRYSTAL STRUCTURE OF VP6, THE MAJOR CAPSID PROTEIN OF GROUP A ROTAVIRUS'''<br />
'''CRYSTAL STRUCTURE OF VP6, THE MAJOR CAPSID PROTEIN OF GROUP A ROTAVIRUS'''<br />
==Overview==
==Overview==
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The structural protein VP6 of rotavirus, an important pathogen responsible, for severe gastroenteritis in children, forms the middle layer in the, triple-layered viral capsid. Here we present the crystal structure of VP6, determined to 2 A resolution and describe its interactions with other, capsid proteins by fitting the atomic model into electron cryomicroscopic, reconstructions of viral particles. VP6, which forms a tight trimer, has, two distinct domains: a distal beta-barrel domain and a proximal, alpha-helical domain, which interact with the outer and inner layer of the, virion, respectively. The overall fold is similar to that of protein VP7, from bluetongue virus, with the subunits wrapping about a central 3-fold, axis. A distinguishing feature of the VP6 trimer is a central Zn(2+) ion, located on the 3-fold molecular axis. The crude atomic model of the middle, layer derived from the fit shows that quasi-equivalence is only partially, obeyed by VP6 in the T = 13 middle layer and suggests a model for the, assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.
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The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis. A distinguishing feature of the VP6 trimer is a central Zn(2+) ion located on the 3-fold molecular axis. The crude atomic model of the middle layer derived from the fit shows that quasi-equivalence is only partially obeyed by VP6 in the T = 13 middle layer and suggests a model for the assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.
==About this Structure==
==About this Structure==
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1QHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_rotavirus Bovine rotavirus] with ZN, CL, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QHD OCA].
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1QHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bovine_rotavirus Bovine rotavirus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QHD OCA].
==Reference==
==Reference==
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[[Category: Mathieu, M.]]
[[Category: Mathieu, M.]]
[[Category: Petitpas, I.]]
[[Category: Petitpas, I.]]
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[[Category: Rey, F.A.]]
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[[Category: Rey, F A.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CA]]
[[Category: CA]]
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[[Category: viral capsid protein]]
[[Category: viral capsid protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:41:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:33 2008''

Revision as of 12:39, 21 February 2008


1qhd, resolution 1.95Å

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CRYSTAL STRUCTURE OF VP6, THE MAJOR CAPSID PROTEIN OF GROUP A ROTAVIRUS

Overview

The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping about a central 3-fold axis. A distinguishing feature of the VP6 trimer is a central Zn(2+) ion located on the 3-fold molecular axis. The crude atomic model of the middle layer derived from the fit shows that quasi-equivalence is only partially obeyed by VP6 in the T = 13 middle layer and suggests a model for the assembly of the 260 VP6 trimers onto the T = 1 viral inner layer.

About this Structure

1QHD is a Single protein structure of sequence from Bovine rotavirus with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion., Mathieu M, Petitpas I, Navaza J, Lepault J, Kohli E, Pothier P, Prasad BV, Cohen J, Rey FA, EMBO J. 2001 Apr 2;20(7):1485-97. PMID:11285213

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