View source for 10ed


==CbrXA SLC5-STAC domains==
<StructureSection load='10ed' size='340' side='right'caption='[[10ed]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[10ed]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=10ED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10ED FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene>, <scene name='pdbligand=R16:HEXADECANE'>R16</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=10ed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10ed OCA], [https://pdbe.org/10ed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10ed RCSB], [https://www.ebi.ac.uk/pdbsum/10ed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10ed ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The CbrA protein is a central regulator of carbon metabolism, biofilm formation, and virulence in Pseudomonas species, but the molecular mechanisms by which CbrA links nutrient sensing to downstream signaling has remained unclear. CbrA is a rare "transceptor" that combines membrane transporter and histidine kinase domains into a single functional polypeptide. The structural basis for histidine recognition and membrane transport, as well as signaling through intracellular histidine kinase domains has remained elusive. Here we determined a cryo-EM structure of CbrA which provides key molecular details of the SLC5-STAC domains in this unusual system. Unexpectedly, the small peptide CbrX encoded upstream of CbrA formed a stable complex with the SLC5 transporter domain, but was not essential for growth of Pseudomonas putida on histidine as a sole carbon source. The cryo-EM structure reveals how histidine binds within the transporter, and molecular dynamics simulations provide insight into proton gradient driven conformational changes that enable histidine transport. These findings define the molecular architecture of key CbrA functional domains, and lay the foundation for developing a comprehensive understanding of coupling between membrane transport and downstream signaling pathways that guide essential physiological traits in Pseudomonas.

Structure and conformational dynamics of the Pseudomonas CbrA transceptor.,Orlando MA, Shah T, Faber MW, Bose S, Orlando BJ Protein Sci. 2026 Sep;35(9):e70775. doi: 10.1002/pro.70775. PMID:42615741<ref>PMID:42615741</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 10ed" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida KT2440]]
[[Category: Bose S]]
[[Category: Chouhan V]]
[[Category: Faber MM]]
[[Category: Orlando BJ]]
[[Category: Orlando MA]]
[[Category: Shah T]]