This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5l35

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:43, 6 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution==
==Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution==
-
<StructureSection load='5l35' size='340' side='right'caption='[[5l35]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
+
<SX load='5l35' size='340' side='right' viewer='molstar' caption='[[5l35]], [[Resolution|resolution]] 2.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5l35]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_phage_sf6 Shigella phage sf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L35 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5l35]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_virus_Sf6 Shigella virus Sf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L35 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.89&#8491;</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=5l35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l35 OCA], [http://pdbe.org/5l35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l35 RCSB], [http://www.ebi.ac.uk/pdbsum/5l35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l35 ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5l35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l35 OCA], [https://pdbe.org/5l35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l35 RCSB], [https://www.ebi.ac.uk/pdbsum/5l35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l35 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q716H0_BPSFV Q716H0_BPSFV]
-
The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as approximately 50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 A resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon-like intercapsomer joints, and abundant beta-sheet-like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic alpha-helix-to-beta-strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.
+
-
 
+
-
Structure of a headful DNA-packaging bacterial virus at 2.9 A resolution by electron cryo-microscopy.,Zhao H, Li K, Lynn AY, Aron KE, Yu G, Jiang W, Tang L Proc Natl Acad Sci U S A. 2017 Mar 20. pii: 201615025. doi:, 10.1073/pnas.1615025114. PMID:28320961<ref>PMID:28320961</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5l35" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
-
</StructureSection>
+
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Shigella phage sf6]]
+
[[Category: Shigella virus Sf6]]
-
[[Category: Tang, L]]
+
[[Category: Tang L]]
-
[[Category: Zhao, H]]
+
[[Category: Zhao H]]
-
[[Category: Phage]]
+
-
[[Category: Sf6]]
+
-
[[Category: Virus]]
+

Current revision

Cryo-EM structure of bacteriophage Sf6 at 2.9 Angstrom resolution

5l35, resolution 2.89Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools