6hc1: Difference between revisions

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'''Unreleased structure'''


The entry 6hc1 is ON HOLD
==Bdellovibrio bacteriovorus DgcB FHA in complex with phosphorylated N-terminal peptide==
<StructureSection load='6hc1' size='340' side='right'caption='[[6hc1]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hc1]] 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=6HC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HC1 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]] 1.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=6hc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hc1 OCA], [https://pdbe.org/6hc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hc1 RCSB], [https://www.ebi.ac.uk/pdbsum/6hc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hc1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6MPU8_BDEBA Q6MPU8_BDEBA]
<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.


Authors: Lovering, A.L., Meek, R.W.
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>


Description: Bdellovibrio bacteriovorus DgcB FHA in complex with phosphorylated N-terminal peptide
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Lovering, A.L]]
<div class="pdbe-citations 6hc1" style="background-color:#fffaf0;"></div>
[[Category: Meek, R.W]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bdellovibrio bacteriovorus HD100]]
[[Category: Large Structures]]
[[Category: Lovering AL]]
[[Category: Meek RW]]
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