View source for 9myr


==Sal-Shy(DUF35) aldolase from Comamonas testosteroni==
<StructureSection load='9myr' size='340' side='right'caption='[[9myr]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9myr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni_KF-1 Comamonas testosteroni KF-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MYR 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9myr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9myr OCA], [https://pdbe.org/9myr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9myr RCSB], [https://www.ebi.ac.uk/pdbsum/9myr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9myr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7X4S8_COMTK B7X4S8_COMTK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aldolases hold potential as biocatalysts for the synthesis of novel steroid pharmaceuticals. The steroid aldolase from Comamonas testosteroni (CtSal) forms a complex with C. testosteroni steroid hydratase (CtShy). CtSal cleaves the C(5) side chain of bile acid thioester steroids, whereas a previously characterized actinobacterial homolog from Thermonospora curvata (TcLtp2) targets the C(3) side chain. We identified Tyr302 and Cys304 as the catalytic residues in CtSal, different from the paired Tyr residues found in TcLtp2. The 1.95 A structure of CtSal bound to the C-terminal domain of unknown function 35 (DUF35) of CtShy (CtShy(DUF35)-CtSal) reveals a central CtSal dimer flanked by two CtShy(DUF35) domains in an alphabetabetaalpha arrangement. CtShy(DUF35) has a unique Cys(3)His(1) (C(3)H(1)) zinc finger that shapes the substrate-binding cleft of CtSal, preventing the binding of the flat cholesterol rings while accommodating the bent rings of bile acids. Phylogenetically, Sals and Ltp2s form separate clades and are distantly related to thiolases. Intriguingly, a Trypanosoma brucei homolog, annotated as a thiolase-like protein (TbSLP), shares the catalytic architecture of CtSal, suggesting an aldolase rather than a thiolase function. This study provides the first detailed characterization of a C(5) side chain steroid aldolase, revealing its unique catalytic features and expanding our understanding of steroid side chain catabolism in Proteobacteria.

Sal is a proteobacterial bile acid aldolase that repurposes key thiolase catalytic residues for retroaldol cleavage of C(5) steroid side chains.,Rolfe N, Schroeter KL, Forrester TJ, Kimber MS, Seah SY J Biol Chem. 2025 Aug;301(8):110439. doi: 10.1016/j.jbc.2025.110439. Epub 2025 , Jul 1. PMID:40609792<ref>PMID:40609792</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9myr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Comamonas testosteroni KF-1]]
[[Category: Large Structures]]
[[Category: Forrester TJB]]
[[Category: Kimber MS]]
[[Category: Rolfe N]]
[[Category: Schroeter KL]]
[[Category: Seah SYK]]