3j0h: Difference between revisions
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[[ | ==Fitting of the bacteriophage phiKZ gp29PR structure into the cryo-EM density map of the phiKZ extended tail sheath== | ||
<StructureSection load='3j0h' size='340' side='right' caption='[[3j0h]], [[Resolution|resolution]] 18.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3j0h]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_phikz Pseudomonas phage phikz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0H FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3spe|3spe]], [[3j0i|3j0i]], [[3hxl|3hxl]], [[3lml|3lml]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j0h RCSB], [http://www.ebi.ac.uk/pdbsum/3j0h PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 A diameter icosahedral head and a 2000 A-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 A resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 A resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4. | |||
Structural conservation of the myoviridae phage tail sheath protein fold.,Aksyuk AA, Kurochkina LP, Fokine A, Forouhar F, Mesyanzhinov VV, Tong L, Rossmann MG Structure. 2011 Dec 7;19(12):1885-94. PMID:22153511<ref>PMID:22153511</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Pseudomonas phage phikz]] | [[Category: Pseudomonas phage phikz]] | ||
[[Category: Aksyuk, A A.]] | [[Category: Aksyuk, A A.]] | ||
Revision as of 13:27, 28 May 2014
Fitting of the bacteriophage phiKZ gp29PR structure into the cryo-EM density map of the phiKZ extended tail sheathFitting of the bacteriophage phiKZ gp29PR structure into the cryo-EM density map of the phiKZ extended tail sheath
Structural highlights
Publication Abstract from PubMedBacteriophage phiKZ is a giant phage that infects Pseudomonas aeruginosa, a human pathogen. The phiKZ virion consists of a 1450 A diameter icosahedral head and a 2000 A-long contractile tail. The structure of the whole virus was previously reported, showing that its tail organization in the extended state is similar to the well-studied Myovirus bacteriophage T4 tail. The crystal structure of a tail sheath protein fragment of phiKZ was determined to 2.4 A resolution. Furthermore, crystal structures of two prophage tail sheath proteins were determined to 1.9 and 3.3 A resolution. Despite low sequence identity between these proteins, all of these structures have a similar fold. The crystal structure of the phiKZ tail sheath protein has been fitted into cryo-electron-microscopy reconstructions of the extended tail sheath and of a polysheath. The structural rearrangement of the phiKZ tail sheath contraction was found to be similar to that of phage T4. Structural conservation of the myoviridae phage tail sheath protein fold.,Aksyuk AA, Kurochkina LP, Fokine A, Forouhar F, Mesyanzhinov VV, Tong L, Rossmann MG Structure. 2011 Dec 7;19(12):1885-94. PMID:22153511[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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