8hdt

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'''Unreleased structure'''
 
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The entry 8hdt is ON HOLD
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==Cyanophage Pam3 capsid asymmetric unit==
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<StructureSection load='8hdt' size='340' side='right'caption='[[8hdt]], [[Resolution|resolution]] 3.17&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8hdt]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_cyanophage Uncultured cyanophage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HDT FirstGlance]. <br>
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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]] 3.17&#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=8hdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hdt OCA], [https://pdbe.org/8hdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hdt RCSB], [https://www.ebi.ac.uk/pdbsum/8hdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hdt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A9E7DT27_9CAUD A0A9E7DT27_9CAUD]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The myophage possesses a contractile tail that penetrates its host cell envelope. Except for investigations on the bacteriophage T4 with a rather complicated structure, the assembly pattern and tail contraction mechanism of myophage remain largely unknown. Here, we present the fine structure of a freshwater Myoviridae cyanophage Pam3, which has an icosahedral capsid of ~680 A in diameter, connected via a three-section neck to an 840-A-long contractile tail, ending with a three-module baseplate composed of only six protein components. This simplified baseplate consists of a central hub-spike surrounded by six wedge heterotriplexes, to which twelve tail fibers are covalently attached via disulfide bonds in alternating upward and downward configurations. In vitro reduction assays revealed a putative redox-dependent mechanism of baseplate assembly and tail sheath contraction. These findings establish a minimal myophage that might become a user-friendly chassis phage in synthetic biology.
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Authors: Yang, F., Jiang, Y.L., Zhou, C.Z.
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Fine structure and assembly pattern of a minimal myophage Pam3.,Yang F, Jiang YL, Zhang JT, Zhu J, Du K, Yu RC, Wei ZL, Kong WW, Cui N, Li WF, Chen Y, Li Q, Zhou CZ Proc Natl Acad Sci U S A. 2023 Jan 24;120(4):e2213727120. doi: , 10.1073/pnas.2213727120. Epub 2023 Jan 19. PMID:36656854<ref>PMID:36656854</ref>
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Description: Cyanophage Pam3 capsid asymmetric unit
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Jiang, Y.L]]
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<div class="pdbe-citations 8hdt" style="background-color:#fffaf0;"></div>
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[[Category: Yang, F]]
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== References ==
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[[Category: Zhou, C.Z]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Uncultured cyanophage]]
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[[Category: Jiang YL]]
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[[Category: Yang F]]
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[[Category: Zhou CZ]]

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Cyanophage Pam3 capsid asymmetric unit

PDB ID 8hdt

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