3qr7
From Proteopedia
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| - | [[ | + | ==Crystal structure of the C-terminal fragment of the bacteriophage P2 membrane-piercing protein gpV== | 
| + | <StructureSection load='3qr7' size='340' side='right' caption='[[3qr7]], [[Resolution|resolution]] 0.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3qr7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p2 Enterobacteria phage p2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QR7 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qr8|3qr8]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10679 Enterobacteria phage P2])</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=3qr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qr7 RCSB], [http://www.ebi.ac.uk/pdbsum/3qr7 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteriophages with contractile tails and the bacterial type VI secretion system have been proposed to use a special protein to create an opening in the host cell membrane during infection. These proteins have a modular architecture but invariably contain an oligonucleotide/oligosaccharide-binding (OB-fold) domain and a long beta-helical C-terminal domain, which initiates the contact with the host cell membrane. Using X-ray crystallography and electron microscopy, we report the atomic structure of the membrane-piercing proteins from bacteriophages P2 and varphi92 and identify the residues that constitute the membrane-attacking apex. Both proteins form compact spikes with a approximately 10A diameter tip that is stabilized by a centrally positioned iron ion bound by six histidine residues. The accumulated data strongly suggest that, in the process of membrane penetration, the spikes are translocated through the lipid bilayer without undergoing major unfolding. | ||
| - | + | Phage pierces the host cell membrane with the iron-loaded spike.,Browning C, Shneider MM, Bowman VD, Schwarzer D, Leiman PG Structure. 2012 Feb 8;20(2):326-39. PMID:22325780<ref>PMID:22325780</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| [[Category: Enterobacteria phage p2]] | [[Category: Enterobacteria phage p2]] | ||
| [[Category: Browning, C.]] | [[Category: Browning, C.]] | ||
Revision as of 05:32, 4 June 2014
Crystal structure of the C-terminal fragment of the bacteriophage P2 membrane-piercing protein gpV
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