1no7

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[[Image:1no7.jpg|left|200px]]
 
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==Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1==
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The line below this paragraph, containing "STRUCTURE_1no7", creates the "Structure Box" on the page.
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<StructureSection load='1no7' size='340' side='right'caption='[[1no7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1no7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NO7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1no7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1no7 OCA], [https://pdbe.org/1no7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1no7 RCSB], [https://www.ebi.ac.uk/pdbsum/1no7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1no7 ProSAT]</span></td></tr>
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{{STRUCTURE_1no7| PDB=1no7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MCP_HHV11 MCP_HHV11] Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.<ref>PMID:8393939</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/1no7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1no7 ConSurf].
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<div style="clear:both"></div>
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'''Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1'''
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human alphaherpesvirus 1]]
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1NO7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO7 OCA].
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[[Category: Large Structures]]
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[[Category: Baker ML]]
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==Reference==
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[[Category: Bowman BR]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12574112 12574112]
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[[Category: Chiu W]]
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[[Category: Human herpesvirus 1]]
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[[Category: Quiocho FA]]
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[[Category: Single protein]]
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[[Category: Rixon FJ]]
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[[Category: Baker, M L.]]
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[[Category: Bowman, B R.]]
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[[Category: Chiu, W.]]
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[[Category: Quiocho, F A.]]
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[[Category: Rixon, F J.]]
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[[Category: Alpha plus beta]]
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[[Category: Folding nucleus]]
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[[Category: Novel fold]]
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[[Category: Viral capsid protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:46:15 2008''
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Current revision

Structure of the Large Protease Resistant Upper Domain of VP5, the Major Capsid Protein of Herpes Simplex Virus-1

PDB ID 1no7

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