7dou

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m (Protected "7dou" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 7dou is ON HOLD
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==Trimeric cement protein structure of Helicobacter pylori bacteriophage KHP40==
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<StructureSection load='7dou' size='340' side='right'caption='[[7dou]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DOU 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&#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=7dou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dou OCA], [https://pdbe.org/7dou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dou RCSB], [https://www.ebi.ac.uk/pdbsum/7dou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dou 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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The acid-stable capsid structures of Helicobacter pylori phages KHP30 and KHP40 are solved at 2.7 and 3.0 A resolutions by cryoelectron microscopy, respectively. The capsids have icosahedral T = 9 symmetry and consist of each 540 copies of 2 structural proteins, a major capsid protein, and a cement protein. The major capsid proteins form 12 pentagonal capsomeres occupying icosahedral vertexes and 80 hexagonal capsomeres located at icosahedral faces and edges. The major capsid protein has a unique protruding loop extending to the neighboring subunit that stabilizes hexagonal capsomeres. Furthermore, the capsid is decorated with trimeric cement proteins with a jelly roll motif. The cement protein trimer sits on the quasi-three-fold axis formed by three major capsid protein capsomeres, thereby enhancing the particle stability by connecting these capsomeres. Sequence and structure comparisons between the related Helicobacter pylori phages suggest a possible mechanism of phage adaptation to the human gastric environment.
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Authors:
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Acid-stable capsid structure of Helicobacter pylori bacteriophage KHP30 by single-particle cryoelectron microscopy.,Kamiya R, Uchiyama J, Matsuzaki S, Murata K, Iwasaki K, Miyazaki N Structure. 2021 Sep 27. pii: S0969-2126(21)00329-4. doi:, 10.1016/j.str.2021.09.001. PMID:34597601<ref>PMID:34597601</ref>
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Description:
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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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<div class="pdbe-citations 7dou" 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: Large Structures]]
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[[Category: Iwasaki K]]
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[[Category: Kamiya R]]
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[[Category: Matsuzaki S]]
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[[Category: Miyazaki N]]
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[[Category: Murata K]]
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[[Category: Uchiyama J]]

Current revision

Trimeric cement protein structure of Helicobacter pylori bacteriophage KHP40

PDB ID 7dou

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