View source for 22zt


==A misfolded structure of an FAD-binding protein CT375==
<StructureSection load='22zt' size='340' side='right'caption='[[22zt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22zt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_trachomatis_D/UW-3/CX Chlamydia trachomatis D/UW-3/CX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22ZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22ZT 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=22zt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22zt OCA], [https://pdbe.org/22zt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22zt RCSB], [https://www.ebi.ac.uk/pdbsum/22zt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22zt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O84380_CHLTR O84380_CHLTR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Misfolded proteins, if not refolded by molecular chaperones, are typically targeted for degradation by cellular quality control systems or tend to aggregate. In the present study, we report a rarely observed crystal structure of a misfolded structure that exists as a stable monomer in solution. The CT375 protein from Chlamydia trachomatis, annotated as a putative d-amino acid dehydrogenase (DAADH), was confirmed to contain the flavin adenine dinucleotide (FAD) through ultraviolet-visible absorption spectroscopy and liquid chromatography-mass spectrometry analyses. However, high-resolution electron density maps excluded the presence of an FAD cofactor bound within the crystallized CT375. This abnormal apo conformation cannot be explained by the loss of FAD during crystallization, as the loop aberrantly occupying the active pocket cannot transition between its current conformation and the FAD-bound conformation observed in homologous oxidoreductases without passing through a two-stranded beta-sheet. It is likely that the interactions between this misfolded loop, instead of FAD, and the active pocket residues contribute to stabilizing the overall fold of CT375 in this misfolded state, and that the misfolded protein, present within the heterogeneous CT375 sample, was fortuitously crystallized. The structure of misfolded CT375 underscores the critical role of the cofactor in correct protein folding and provides a valuable model for advancing the understanding of protein misfolding and its potential mechanisms underlying protein dysfunction.

Crystallographic analysis of a putative FAD-dependent oxidoreductase identifies a potentially misfolded apo structure in a soluble monomeric state.,Xu J, Han L, Qi H, Han Y, Chen B, Ju Y, Zhou H J Struct Biol. 2026 May 27;218(3):108331. doi: 10.1016/j.jsb.2026.108331. PMID:42208745<ref>PMID:42208745</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 22zt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydia trachomatis D/UW-3/CX]]
[[Category: Large Structures]]
[[Category: Han L]]
[[Category: Ju Y]]
[[Category: Xu J]]
[[Category: Zhou H]]