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'''Unreleased structure'''


The entry 9vli is ON HOLD
==Crystal structure of Bacillus subtilis DegQ S25L mutant==
<StructureSection load='9vli' size='340' side='right'caption='[[9vli]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vli]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VLI 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]] 1.6&#8491;</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=9vli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vli OCA], [https://pdbe.org/9vli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vli RCSB], [https://www.ebi.ac.uk/pdbsum/9vli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vli ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEGQ_BACSU DEGQ_BACSU] Stimulates the phosphotransfer from phospho-DegS to DegU. Affects protease and levansucrose production.<ref>PMID:17850253</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacillus subtilis DegQ is a 46-amino-acid regulatory protein involved in the DegS-DegU two-component system. DegQ promotes the phosphorylation of DegU by DegS, switching the function of DegU from competence to the induction of poly-gamma-glutamate production. To elucidate its structural role, we determined the crystal structures of wild-type DegQ and its mutant DegQS25L. Each DegQ monomer folds into a single alpha-helix, and four monomers assemble into a tetramer characterized by a four-helix coiled-coil structure. Within the tetramer, two adjacent helices are oriented in the same direction, while the other two are oriented oppositely, forming a pseudo-twofold symmetric arrangement. The mutant form displays disrupted symmetry due to altered helix packing, which is caused by shifts in the coiled-coil heptad register induced by the mutation. Structural predictions using AlphaFold3 suggest that DegQ likely binds to the N-terminal helix bundle of DegS, either as a dimer or as individual monomers. These findings provide structural insight into DegQ oligomerization and its potential role in modulating DegS autophosphorylation and DegU binding.


Authors:  
Tetrameric structure of Bacillus subtilis DegQ and its predicted interaction with the DegS-DegU two-component system.,Fujimoto Z, Kishine N, Saitou K, Kimura K Acta Crystallogr F Struct Biol Commun. 2025 Oct 1. doi: , 10.1107/S2053230X25007903. PMID:40937771<ref>PMID:40937771</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9vli" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Fujimoto Z]]
[[Category: Kimura K]]
[[Category: Kishine N]]
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