6oma

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(New page: '''Unreleased structure''' The entry 6oma is ON HOLD Authors: Huet, A., Duda, R.L., Boulanger, P., Conway, J.F. Description: non-decorated head of the phage T5 [[Category: Unreleased S...)
Current revision (09:24, 20 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6oma is ON HOLD
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==non-decorated head of the phage T5==
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<SX load='6oma' size='340' side='right' viewer='molstar' caption='[[6oma]], [[Resolution|resolution]] 7.20&Aring;' scene=''>
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Authors: Huet, A., Duda, R.L., Boulanger, P., Conway, J.F.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6oma]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T5 Escherichia virus T5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OMA FirstGlance]. <br>
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Description: non-decorated head of the phage T5
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.2&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=6oma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oma OCA], [https://pdbe.org/6oma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oma RCSB], [https://www.ebi.ac.uk/pdbsum/6oma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oma ProSAT]</span></td></tr>
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[[Category: Boulanger, P]]
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</table>
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[[Category: Duda, R.L]]
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== Function ==
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[[Category: Huet, A]]
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[https://www.uniprot.org/uniprot/CAPSD_BPT5 CAPSD_BPT5] Major capsid protein that self-associates to form 120 hexamers and 11 pentamers, building the T=13 icosahedral capsid which about 860 Angstroms in diameter. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function. The capsid gains its final stability through the reorganization of the subunits that takes place upon expansion. DNA encapsidation through the portal triggers capsid expansion and the binding of the decoration protein to the capsid exterior.<ref>PMID:20573812</ref> <ref>PMID:23500494</ref> <ref>PMID:26616586</ref>
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[[Category: Conway, J.F]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Escherichia virus T5]]
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[[Category: Large Structures]]
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[[Category: Boulanger P]]
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[[Category: Conway JF]]
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[[Category: Duda RL]]
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[[Category: Huet A]]

Current revision

non-decorated head of the phage T5

6oma, resolution 7.20Å

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