6cgv

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<StructureSection load='6cgv' size='340' side='right' caption='[[6cgv]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<StructureSection load='6cgv' size='340' side='right' caption='[[6cgv]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6cgv]] is a 21 chain structure. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4cwu 4cwu] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsz 1vsz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6cgv]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Ade05 Ade05]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4cwu 4cwu] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsz 1vsz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CGV FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b1t|6b1t]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b1t|6b1t]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28285 ADE05]), L2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28285 ADE05]), L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28285 ADE05]), IX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28285 ADE05]), L4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28285 ADE05])</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=6cgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgv OCA], [http://pdbe.org/6cgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgv RCSB], [http://www.ebi.ac.uk/pdbsum/6cgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgv ProSAT]</span></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=6cgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgv OCA], [http://pdbe.org/6cgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgv RCSB], [http://www.ebi.ac.uk/pdbsum/6cgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Human adenoviruses (HAdVs) cause acute respiratory, ocular, and gastroenteric diseases and are also frequently used as gene and vaccine delivery vectors. Unlike the archetype human adenovirus C5 (HAdV-C5), human adenovirus D26 (HAdV-D26) belongs to species-D HAdVs, which target different cellular receptors, and is differentially recognized by immune surveillance mechanisms. HAdV-D26 is being championed as a lower seroprevalent vaccine and oncolytic vector in preclinical and human clinical studies. To understand the molecular basis for their distinct biological properties and independently validate the structures of minor proteins, we determined the first structure of species-D HAdV at 3.7 A resolution by cryo-electron microscopy. All the hexon hypervariable regions (HVRs), including HVR1, have been identified and exhibit a distinct organization compared to those of HAdV-C5. Despite the differences in the arrangement of helices in the coiled-coil structures, protein IX molecules form a continuous hexagonal network on the capsid exterior. In addition to the structurally conserved region (3 to 300) of IIIa, we identified an extra helical domain comprising residues 314 to 390 that further stabilizes the vertex region. Multiple (two to three) copies of the cleaved amino-terminal fragment of protein VI (pVIn) are observed in each hexon cavity, suggesting that there could be &gt;/=480 copies of VI present in HAdV-D26. In addition, a localized asymmetric reconstruction of the vertex region provides new details of the three-pronged "claw hold" of the trimeric fiber and its interactions with the penton base. These observations resolve the previous conflicting assignments of the minor proteins and suggest the likely conservation of their organization across different HAdVs.
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We report the revised crystal structure of a pseudo-typed human adenovirus at 3.8-A resolution that is consistent with the atomic models of minor proteins determined by cryo-electron microscopy. The diffraction data from multiple crystals were rescaled and merged to increase the data completeness. The densities for the minor proteins were initially identified in the phase-refined omit maps that were further improved by the phases from docked poly-alanine models to build atomic structures. While the trimeric fiber molecules are disordered due to flexibility and imposition of 5-fold symmetry, the remaining major capsid proteins hexon and penton base are clearly ordered, with the exception of hypervariable region 1 of hexons, the RGD containing loop, and the N-termini of the penton base. The exterior minor protein IX together with the interior minor proteins IIIa and VIII stabilizes the adenovirus virion. A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered. While the triskelion substructures formed by the N-termini of IX conform to excellent quasi 3-fold symmetry, the tetrameric coiled-coils formed by the C-termini and organized in parallel and anti-parallel arrangement do not exhibit any quasi-symmetry. This observation also conveys the pitfalls of using the quasi-equivalence as validation criteria for the structural analysis of extended (non-modular) capsid proteins such as IX. Together, these results remedy certain discrepancies in the previous X-ray model in agreement with the cryo-electron microscopy models.
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Cryo-EM structure of human adenovirus D26 reveals the conservation of structural organization among human adenoviruses.,Yu X, Veesler D, Campbell MG, Barry ME, Asturias FJ, Barry MA, Reddy VS Sci Adv. 2017 May 10;3(5):e1602670. doi: 10.1126/sciadv.1602670. eCollection 2017, May. PMID:28508067<ref>PMID:28508067</ref>
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Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes.,Kundhavai Natchiar S, Venkataraman S, Mullen TM, Nemerow GR, Reddy VS J Mol Biol. 2018 Aug 17. pii: S0022-2836(18)30639-9. doi:, 10.1016/j.jmb.2018.08.011. PMID:30121295<ref>PMID:30121295</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ade05]]
[[Category: Natchiar, S K]]
[[Category: Natchiar, S K]]
[[Category: Nemerow, G R]]
[[Category: Nemerow, G R]]

Revision as of 10:27, 5 September 2018

Revised crystal structure of human adenovirus

6cgv, resolution 3.80Å

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