7dn2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Acidic stable capsid structure of Helicobacter pylori bacteriophage KHP30== | |
| + | <SX load='7dn2' size='340' side='right' viewer='molstar' caption='[[7dn2]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7dn2]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_phage_KHP30 Helicobacter phage KHP30]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DN2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dn2 OCA], [https://pdbe.org/7dn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dn2 RCSB], [https://www.ebi.ac.uk/pdbsum/7dn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dn2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ORF14_BPKHP ORF14_BPKHP] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7dn2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Helicobacter phage KHP30]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Iwasaki K]] | ||
| + | [[Category: Kamiya R]] | ||
| + | [[Category: Matsuzaki S]] | ||
| + | [[Category: Miyazaki N]] | ||
| + | [[Category: Murata K]] | ||
| + | [[Category: Uchiyama J]] | ||
Current revision
Acidic stable capsid structure of Helicobacter pylori bacteriophage KHP30
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