View source for 25xa


==Crystal structure of bacterial DUSP from Candidatus Chlorohelix allophototropha==
<StructureSection load='25xa' size='340' side='right'caption='[[25xa]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[25xa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexia Chloroflexia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=25XA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=25XA 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=25xa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=25xa OCA], [https://pdbe.org/25xa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=25xa RCSB], [https://www.ebi.ac.uk/pdbsum/25xa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=25xa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8T7M2Z3_9CHLR A0A8T7M2Z3_9CHLR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dual specificity phosphatases (DUSPs) are a subfamily of protein tyrosine phosphatases that regulate diverse cellular processes through dephosphorylation of phosphorylated substrates. DUSPs are commonly found in eukaryotes, bacteria, archaea, and viruses. However, structural and biochemical characterization of bacterial DUSP remains limited, as only one bacterial DUSP has been identified thus far. In this study, we investigated a novel putative bacterial DUSP from Candidatus Chlorohelix allophototropha, referred to as CCaDUSP. The crystal structure of CCaDUSP showed the presence of a well-conserved catalytic motif with a characteristic phosphate-binding loop. Biochemical analyses further confirmed that CCaDUSP exhibits phosphatase activity and contains dual general acid/base residues, both of which contribute to its enzymatic activity. These findings not only represent the first characterization of a novel bacterial DUSP with dual general acid/base residues but also provide a foundation for understanding the diversity of DUSP proteins in bacteria.

Structural and biochemical analyses of a novel bacterial dual specificity phosphatase from Candidatus Chlorohelix allophototropha.,Jung S, Park SH, Choi JS, Shin HC, Kim SJ, Ku B J Microbiol. 2026 Jul;64(7):e2604025. doi: 10.71150/jm.2604025. Epub 2026 Jul 16. PMID:42457432<ref>PMID:42457432</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 25xa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chloroflexia]]
[[Category: Large Structures]]
[[Category: Jung S]]
[[Category: Ku B]]