8onf: Difference between revisions
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The | ==Crystal structure of Bdellovibrio bacteriovorus Bd2439 fibre C-terminal domains with ethylene glycol== | ||
<StructureSection load='8onf' size='340' side='right'caption='[[8onf]], [[Resolution|resolution]] 1.53Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8onf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ONF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ONF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=8onf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8onf OCA], [https://pdbe.org/8onf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8onf RCSB], [https://www.ebi.ac.uk/pdbsum/8onf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8onf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6MKF5_BDEBA Q6MKF5_BDEBA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Predatory bacteria, like the model endoperiplasmic bacterium Bdellovibrio bacteriovorus, show several adaptations relevant to their requirements for locating, entering and killing other bacteria. The mechanisms underlying prey recognition and handling remain obscure. Here we use complementary genetic, microscopic and structural methods to address this deficit. During invasion, the B. bacteriovorus protein CpoB concentrates into a vesicular compartment that is deposited into the prey periplasm. Proteomic and structural analyses of vesicle contents reveal several fibre-like proteins, which we name the mosaic adhesive trimer (MAT) superfamily, and show localization on the predator surface before prey encounter. These dynamic proteins indicate a variety of binding capabilities, and we confirm that one MAT member shows specificity for surface glycans from a particular prey. Our study shows that the B. bacteriovorus MAT protein repertoire enables a broad means for the recognition and handling of diverse prey epitopes encountered during bacterial predation and invasion. | |||
Bdellovibrio bacteriovorus uses chimeric fibre proteins to recognize and invade a broad range of bacterial hosts.,Caulton SG, Lambert C, Tyson J, Radford P, Al-Bayati A, Greenwood S, Banks EJ, Clark C, Till R, Pires E, Sockett RE, Lovering AL Nat Microbiol. 2024 Jan;9(1):214-227. doi: 10.1038/s41564-023-01552-2. Epub 2024 , Jan 4. PMID:38177296<ref>PMID:38177296</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8onf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bdellovibrio bacteriovorus HD100]] | |||
[[Category: Large Structures]] | |||
[[Category: Caulton SG]] | |||
[[Category: Lovering AL]] | |||