View source for 5cea


==Bd3460 Immunity Protein from Bdellovibrio bacteriovorus==
<StructureSection load='5cea' size='340' side='right'caption='[[5cea]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cea]] is a 5 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=5CEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CEA FirstGlance]. <br>
</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=5cea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cea OCA], [https://pdbe.org/5cea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cea RCSB], [https://www.ebi.ac.uk/pdbsum/5cea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cea ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6MHS9_BDEBA Q6MHS9_BDEBA] 
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== Publication Abstract from PubMed ==
Predatory Bdellovibrio bacteriovorus are natural antimicrobial organisms, killing other bacteria by whole-cell invasion. Self-protection against prey-metabolizing enzymes is important for the evolution of predation. Initial prey entry involves the predator's peptidoglycan DD-endopeptidases, which decrosslink cell walls and prevent wasteful entry by a second predator. Here we identify and characterize a self-protection protein from B. bacteriovorus, Bd3460, which displays an ankyrin-based fold common to intracellular pathogens of eukaryotes. Co-crystal structures reveal Bd3460 complexation of dual targets, binding a conserved epitope of each of the Bd3459 and Bd0816 endopeptidases. Complexation inhibits endopeptidase activity and cell wall decrosslinking in vitro. Self-protection is vital - DeltaBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morphology, and lose predatory capacity and cellular integrity. Our analysis provides the first mechanistic examination of self-protection in Bdellovibrio, documents protection-multiplicity for products of two different genomic loci, and reveals an important evolutionary adaptation to an invasive predatory bacterial lifestyle.

Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus.,Lambert C, Cadby IT, Till R, Bui NK, Lerner TR, Hughes WS, Lee DJ, Alderwick LJ, Vollmer W, Sockett ER, Lovering AL Nat Commun. 2015 Dec 2;6:8884. doi: 10.1038/ncomms9884. PMID:26626559<ref>PMID:26626559</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cea" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bdellovibrio bacteriovorus HD100]]
[[Category: Large Structures]]
[[Category: Cadby IT]]
[[Category: Lambert C]]
[[Category: Lovering AL]]
[[Category: Sockett RE]]