7s78
From Proteopedia
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| - | ==== | + | ==Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation== |
| - | <StructureSection load='7s78' size='340' side='right'caption='[[7s78]]' scene=''> | + | <StructureSection load='7s78' size='340' side='right'caption='[[7s78]], [[Resolution|resolution]] 3.72Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7s78]] is a 31 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_adenovirus_5 Human adenovirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S78 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7s78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s78 OCA], [https://pdbe.org/7s78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s78 RCSB], [https://www.ebi.ac.uk/pdbsum/7s78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s78 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.72Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7s78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s78 OCA], [https://pdbe.org/7s78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s78 RCSB], [https://www.ebi.ac.uk/pdbsum/7s78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s78 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CAPSH_ADE05 CAPSH_ADE05] Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Maturation of adenoviruses is distinguished by proteolytic processing of several interior minor capsid proteins and core proteins by the adenoviral protease and subsequent reorganization of adenovirus core. We report the results derived from the icosahedrally averaged cryo-EM structure of a cell entry defective form of adenovirus, designated ts1, at a resolution of 3.7 A as well as of the localized reconstructions of unique hexons and penton base. The virion structure revealed the structures and organization of precursors of minor capsid proteins, pIIIa, pVI and pVIII, which are closely associated with the hexons on the capsid interior. In addition to a well-ordered helical domain (a.a. 310-397) of pIIIa, highlights of the structure include the precursors of VIII display significantly different structures near the cleavage sites. Moreover, we traced residues 4-96 of the membrane lytic protein (pVI) that includes an amphipathic helix occluded deep in the hexon cavity suggesting the possibility of co-assembly of hexons with the precursors of VI. In addition, we observe a second copy of pVI ordered up to residue L40 in the peripentonal hexons and a few fragments of density corresponding to 2nd and 3rd copies of pVI in other hexons. However, we see no evidence of precursors of VII binding in the hexon cavity. These findings suggest the possibility that differently bound pVI molecules undergo processing at the N-terminal cleavage sites at varying efficiencies, subsequently creating competition between the cleaved and uncleaved forms of VI, followed by reorganization, processing, and release of VI molecules from the hexon cavities. | ||
| + | |||
| + | Structure of a Cell Entry Defective Human Adenovirus Provides Insights into Precursor Proteins and Capsid Maturation.,Yu X, Mullen TM, Abrishami V, Huiskonen JT, Nemerow GR, Reddy VS J Mol Biol. 2022 Jan 30;434(2):167350. doi: 10.1016/j.jmb.2021.167350. Epub 2021 , Nov 10. PMID:34774568<ref>PMID:34774568</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7s78" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human adenovirus 5]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Reddy VS]] |
| + | [[Category: Yu X]] | ||
Current revision
Structure of a cell-entry defective human adenovirus provides insights into precursor proteins and capsid maturation
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