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| | <StructureSection load='5ceb' size='340' side='right'caption='[[5ceb]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='5ceb' size='340' side='right'caption='[[5ceb]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ceb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CEB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ceb]] is a 2 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=5CEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CEB FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bd3459 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></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=5ceb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ceb OCA], [https://pdbe.org/5ceb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ceb RCSB], [https://www.ebi.ac.uk/pdbsum/5ceb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ceb ProSAT]</span></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=5ceb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ceb OCA], [http://pdbe.org/5ceb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ceb RCSB], [http://www.ebi.ac.uk/pdbsum/5ceb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ceb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6MHT0_BDEBA Q6MHT0_BDEBA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bdeba]] | + | [[Category: Bdellovibrio bacteriovorus HD100]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
| + | [[Category: Cadby IT]] |
| - | [[Category: Cadby, I T]] | + | [[Category: Lambert C]] |
| - | [[Category: Lambert, C]] | + | [[Category: Lovering AL]] |
| - | [[Category: Lovering, A L]] | + | [[Category: Sockett RE]] |
| - | [[Category: Sockett, R E]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Transpeptidase]]
| + | |
| Structural highlights
Function
Q6MHT0_BDEBA
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lambert C, Cadby IT, Till R, Bui NK, Lerner TR, Hughes WS, Lee DJ, Alderwick LJ, Vollmer W, Sockett ER, Lovering AL. Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nat Commun. 2015 Dec 2;6:8884. doi: 10.1038/ncomms9884. PMID:26626559 doi:http://dx.doi.org/10.1038/ncomms9884
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