4uw8
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Structure of the carboxy-terminal domain of the bacteriophage T5 L- shaped tail fiber with its intra-molecular chaperone domain== |
| + | <StructureSection load='4uw8' size='340' side='right' caption='[[4uw8]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uw8]] is a 9 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UW8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UW8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uw7|4uw7]]</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=4uw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uw8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uw8 RCSB], [http://www.ebi.ac.uk/pdbsum/4uw8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FIBL_BPT5 FIBL_BPT5]] Assembles together with p132 to form the three L-shaped long tail fibers that recognize the host lipopolysaccharides that serve as adhesion receptor for virus entry. P132 makes the proximal part and pb8 the distal part that binds to the host cell surface. The L-shaped long tail fibers are attached to a collar structure at the junction between the tail tube and the conical tail tip. Each fiber consists of a thin proximal rod of about 30 nm connected by a hinge to a thicker distal part of about 47 nm.<ref>PMID:24198424</ref> <ref>PMID:7045389</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tails of bacteriophage T5 (a member of the Siphoviridae family) were studied by electron microscopy. For the distal parts of the L-shaped tail fibres, which are involved in host cell receptor binding, a low-resolution volume was calculated. Several C-terminal fragments of the fibre were expressed and purified. Crystals of two of them were obtained that belonged to space groups P63 and R32 and diffracted synchrotron radiation to 2.3 and 2.9 A resolution, respectively. A single-wavelength anomalous dispersion data set to 2.5 A resolution was also collected from a selenomethionine-derivatized crystal of one of the fragments, which belonged to space group C2. | ||
| - | + | Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre.,Garcia-Doval C, Luque D, Caston JR, Boulanger P, van Raaij MJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1363-7. doi:, 10.1107/S1744309113028959. Epub 2013 Nov 28. PMID:24316831<ref>PMID:24316831</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Boulanger, P]] | [[Category: Boulanger, P]] | ||
| - | [[Category: | + | [[Category: Caston, J R]] |
[[Category: Garcia-Doval, C]] | [[Category: Garcia-Doval, C]] | ||
| - | [[Category: | + | [[Category: Llamas-Saizd, A L]] |
[[Category: Luque, D]] | [[Category: Luque, D]] | ||
| - | [[Category: | + | [[Category: Oteroc, J M]] |
| - | [[Category: | + | [[Category: Raaij, M J.van]] |
| + | [[Category: Bacterial viruse]] | ||
| + | [[Category: Caudovirale]] | ||
| + | [[Category: Infection]] | ||
| + | [[Category: Siphoviridae]] | ||
| + | [[Category: Viral protein]] | ||
Revision as of 20:01, 5 August 2015
Structure of the carboxy-terminal domain of the bacteriophage T5 L- shaped tail fiber with its intra-molecular chaperone domain
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