6b43

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{{Large structure}}
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==CryoEM structure and atomic model of the Kaposi's sarcoma-associated herpesvirus capsid==
==CryoEM structure and atomic model of the Kaposi's sarcoma-associated herpesvirus capsid==
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<StructureSection load='6b43' size='340' side='right' caption='[[6b43]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
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<StructureSection load='6b43' size='340' side='right'caption='[[6b43]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6b43]] is a 46 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j9a 3j9a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B43 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6b43]] is a 46 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3j9a 3j9a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B43 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6b43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b43 OCA], [http://pdbe.org/6b43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b43 RCSB], [http://www.ebi.ac.uk/pdbsum/6b43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b43 ProSAT]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6b43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b43 OCA], [http://pdbe.org/6b43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b43 RCSB], [http://www.ebi.ac.uk/pdbsum/6b43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b43 ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/C7E5A9_HHV8 C7E5A9_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04019] [[http://www.uniprot.org/uniprot/D0UZN7_HHV8 D0UZN7_HHV8]] 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.[HAMAP-Rule:MF_04016] [[http://www.uniprot.org/uniprot/Q76RF6_HHV8 Q76RF6_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04018] [[http://www.uniprot.org/uniprot/Q76RF4_HHV8 Q76RF4_HHV8]] Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly.[HAMAP-Rule:MF_04022]
[[http://www.uniprot.org/uniprot/C7E5A9_HHV8 C7E5A9_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04019] [[http://www.uniprot.org/uniprot/D0UZN7_HHV8 D0UZN7_HHV8]] 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.[HAMAP-Rule:MF_04016] [[http://www.uniprot.org/uniprot/Q76RF6_HHV8 Q76RF6_HHV8]] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.[HAMAP-Rule:MF_04018] [[http://www.uniprot.org/uniprot/Q76RF4_HHV8 Q76RF4_HHV8]] Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly.[HAMAP-Rule:MF_04022]
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</StructureSection>
</StructureSection>
[[Category: Human herpesvirus 8]]
[[Category: Human herpesvirus 8]]
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[[Category: Large Structures]]
[[Category: Dai, X H]]
[[Category: Dai, X H]]
[[Category: Gong, D Y]]
[[Category: Gong, D Y]]

Revision as of 08:16, 27 November 2019

CryoEM structure and atomic model of the Kaposi's sarcoma-associated herpesvirus capsid

PDB ID 6b43

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