5ceb: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus, K38M form== | ==Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus, K38M form== | ||
<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. 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 [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> | ||
</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> | </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> | ||
<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]</span></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'>[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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 19: | Line 21: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bdeba]] | |||
[[Category: Large Structures]] | |||
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
[[Category: Cadby, I T]] | [[Category: Cadby, I T]] | ||
Revision as of 14:34, 27 March 2020
Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus, K38M formBd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus, K38M form
Structural highlights
Publication Abstract from PubMedPredatory 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
|
| ||||||||||||||||||