View source for 9nxl


==Crystal structure of steroid aldehyde dehydrogenase (Sad) from Caldimonas tepidiphilia==
<StructureSection load='9nxl' size='340' side='right'caption='[[9nxl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9nxl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldimonas_tepidiphila Caldimonas tepidiphila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9NXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9NXL 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAF:S-DIMETHYLARSINOYL-CYSTEINE'>CAF</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=9nxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9nxl OCA], [https://pdbe.org/9nxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9nxl RCSB], [https://www.ebi.ac.uk/pdbsum/9nxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9nxl ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The steroid aldehyde dehydrogenase (Sad) from Proteobacteria is a class 3 aldehyde dehydrogenase (ALDH3) that catalyzes the oxidation of C(3) steroid side chain aldehydes during bile acid catabolism. The 1.8 A structure of the enzyme revealed an expanded active site that was able to accommodate bulky steroids, including bile acid intermediates and cholesterol derivatives, with minimal selectivity for ring-conformation or hydroxylation. Sad can utilize both NAD(+) and NADP(+) as coenzymes, likely due to a truncated N-terminus and a flexible Glu149 residue, which can avoid steric and electrostatic repulsion with the 2'-phosphate of NADP(+) while retaining the ability to hydrogen bond to the C2'-OH of NAD(+). Sad was over 1000-fold more specific for steroid aldehyde substrates than for smaller molecules such as benzaldehyde. Structural comparison with the homologousPseudomonas putida benzaldehyde dehydrogenase (PpBADH) suggested residues that might contribute to the ability of Sad to utilize bulky steroid substrates. Replacement of these residues in an F400A/L125T PpBADH double-variant resulted in a approximately 39-fold increase in catalytic efficiency toward steroid aldehyde compared with the wild-type enzyme. This study advances our understanding of the molecular determinants of substrate specificity within the ALDH3 family and lays the groundwork for biocatalytic applications of steroid aldehyde dehydrogenases in the production of steroid pharmaceuticals and the bioremediation of steroidal pollutants.

Sad from Proteobacteria is a Structurally Distinct ALDH3 Enzyme Specialized for the Oxidation of Steroidal Aldehydes.,Rolfe N, Myskiw D, Patton MT, Forrester TJB, Kimber MS, Seah SYK Biochemistry. 2025 Sep 2;64(17):3735-3744. doi: 10.1021/acs.biochem.5c00213. Epub , 2025 Aug 18. PMID:40825534<ref>PMID:40825534</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 9nxl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caldimonas tepidiphila]]
[[Category: Large Structures]]
[[Category: Forrester TJB]]
[[Category: Kimber MS]]
[[Category: Myskiw D]]
[[Category: Patton MT]]
[[Category: Rolfe N]]
[[Category: Seah SYK]]