6hc0: Difference between revisions
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<StructureSection load='6hc0' size='340' side='right'caption='[[6hc0]], [[Resolution|resolution]] 1.87Å' scene=''> | <StructureSection load='6hc0' size='340' side='right'caption='[[6hc0]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6hc0]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HC0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HC0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6hc0]] is a 5 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=6HC0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HC0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hbz|6hbz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hbz|6hbz]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bd0742 ([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=6hc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hc0 OCA], [http://pdbe.org/6hc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hc0 RCSB], [http://www.ebi.ac.uk/pdbsum/6hc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hc0 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=6hc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hc0 OCA], [http://pdbe.org/6hc0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hc0 RCSB], [http://www.ebi.ac.uk/pdbsum/6hc0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hc0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial second messenger cyclic-di-GMP is a widespread, prominent effector of lifestyle change. An example of this occurs in the predatory bacterium Bdellovibrio bacteriovorus, which cycles between free-living and intraperiplasmic phases after entering (and killing) another bacterium. The initiation of prey invasion is governed by DgcB (GGDEF enzyme) that produces cyclic-di-GMP in response to an unknown stimulus. Here, we report the structure of DgcB, and demonstrate that the GGDEF and sensory forkhead-associated (FHA) domains form an asymmetric dimer. Our structures indicate that the FHA domain is a consensus phosphopeptide sensor, and that the ligand for activation is surprisingly derived from the N-terminal region of DgcB itself. We confirm this hypothesis by determining the structure of a FHA:phosphopeptide complex, from which we design a constitutively-active mutant (confirmed via enzyme assays). Our results provide an understanding of the stimulus driving DgcB-mediated prey invasion and detail a unique mechanism of GGDEF enzyme regulation. | |||
Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio.,Meek RW, Cadby IT, Moynihan PJ, Lovering AL Nat Commun. 2019 Sep 9;10(1):4086. doi: 10.1038/s41467-019-12051-6. PMID:31501441<ref>PMID:31501441</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6hc0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bdeba]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lovering, A L]] | [[Category: Lovering, A L]] | ||
Latest revision as of 10:52, 6 November 2019
Bdellovibrio bacteriovorus DgcB FHA domain, tail complexBdellovibrio bacteriovorus DgcB FHA domain, tail complex
Structural highlights
Publication Abstract from PubMedThe bacterial second messenger cyclic-di-GMP is a widespread, prominent effector of lifestyle change. An example of this occurs in the predatory bacterium Bdellovibrio bacteriovorus, which cycles between free-living and intraperiplasmic phases after entering (and killing) another bacterium. The initiation of prey invasion is governed by DgcB (GGDEF enzyme) that produces cyclic-di-GMP in response to an unknown stimulus. Here, we report the structure of DgcB, and demonstrate that the GGDEF and sensory forkhead-associated (FHA) domains form an asymmetric dimer. Our structures indicate that the FHA domain is a consensus phosphopeptide sensor, and that the ligand for activation is surprisingly derived from the N-terminal region of DgcB itself. We confirm this hypothesis by determining the structure of a FHA:phosphopeptide complex, from which we design a constitutively-active mutant (confirmed via enzyme assays). Our results provide an understanding of the stimulus driving DgcB-mediated prey invasion and detail a unique mechanism of GGDEF enzyme regulation. Structural basis for activation of a diguanylate cyclase required for bacterial predation in Bdellovibrio.,Meek RW, Cadby IT, Moynihan PJ, Lovering AL Nat Commun. 2019 Sep 9;10(1):4086. doi: 10.1038/s41467-019-12051-6. PMID:31501441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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