5wk1

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'''Unreleased structure'''
 
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The entry 5wk1 is ON HOLD until Paper Publication
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==Structure of the major capsid protein and the capsid stabilizing protein of the marine siphovirus TW1==
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<StructureSection load='5wk1' size='340' side='right' caption='[[5wk1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wk1]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudoalteromonas_phage_tw1 Pseudoalteromonas phage tw1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WK1 FirstGlance]. <br>
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</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=5wk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wk1 OCA], [http://pdbe.org/5wk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wk1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wk1 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Marine bacteriophage TW1 belongs to the Siphoviridae family and infects Pseudoalteromonas phenolica. Mass spectrometry analysis has identified 16 different proteins in the TW1 virion. Functions of most of these proteins have been predicted by bioinformatic methods. A 3.6 A resolution cryoelectron microscopy map of the icosahedrally averaged TW1 head showed the atomic structures of the major capsid protein, gp57( *), and the capsid-stabilizing protein, gp56. The gp57( *) structure is similar to that of the phage HK97 capsid protein. The gp56 protein has two domains, each having folds similar to that of the N-terminal part of phage lambda gpD, indicating a common ancestry. The first gp56 domain clamps adjacent capsomers together, whereas the second domain is required for trimerization. A 6-fold-averaged reconstruction of the distal part of the tail showed that TW1 has six tail spikes, which are unusual for siphophages but are similar to the podophages P22 and Sf6, suggesting a common evolutionary origin of these spikes.
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Authors: Wang, Z., Rossmann, M.G.
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Structure of the Marine Siphovirus TW1: Evolution of Capsid-Stabilizing Proteins and Tail Spikes.,Wang Z, Hardies SC, Fokine A, Klose T, Jiang W, Cho BC, Rossmann MG Structure. 2017 Dec 26. pii: S0969-2126(17)30400-8. doi:, 10.1016/j.str.2017.12.001. PMID:29290487<ref>PMID:29290487</ref>
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Description: Structure of the major capsid protein and the capsid stabilizing protein of the marine siphovirus TW1
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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: Rossmann, M.G]]
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<div class="pdbe-citations 5wk1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Pseudoalteromonas phage tw1]]
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[[Category: Rossmann, M G]]
[[Category: Wang, Z]]
[[Category: Wang, Z]]
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[[Category: Capsid stabilizing protein]]
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[[Category: Decoration protein]]
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[[Category: Hk 97 fold]]
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[[Category: Major capsid protein]]
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[[Category: Virus]]

Revision as of 06:55, 17 January 2018

Structure of the major capsid protein and the capsid stabilizing protein of the marine siphovirus TW1

5wk1, resolution 3.60Å

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