9w7a: Difference between revisions
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==Crystal structure of L-galactose dehydrogenase from Luteolibacter sp. strain LG18 in complex with L-glucose and NADP+== | |||
<StructureSection load='9w7a' size='340' side='right'caption='[[9w7a]], [[Resolution|resolution]] 1.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9w7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Luteolibacter_sp._LG18 Luteolibacter sp. LG18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9W7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9W7A 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]] 1.56Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=Z8T:beta-L-glucopyranose'>Z8T</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=9w7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9w7a OCA], [https://pdbe.org/9w7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9w7a RCSB], [https://www.ebi.ac.uk/pdbsum/9w7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9w7a ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of l-galactose dehydrogenase (LGDH) with l-glucose dehydrogenase activity from Luteolibacter sp. strain LG18 (Lu-LGDH) was determined in complex with l-galactose or l-glucose and NADP(+). This structural analysis identified key residues involved in substrate binding, and alanine-substituted mutants demonstrated the roles of these residues, including Tyr56, acting as potential general base within the catalytic tetrad. Unlike plant enzymes that show a preference for NAD(+), Lu-LGDH exhibits a marked preference for NADP(+) as a cofactor. This preference was attributed to the interaction of the phosphate group with Arg28, Thr269, and Asn274. The binding mode of l-glucose was similar to that of l-galactose. The C4 hydroxyl group (the structural difference between these pyranoses) was not used for substrate binding, which explains the dual activity of the enzyme. Furthermore, among the substrate-binding residues that were mutated, Arg308, which is not conserved among LGDHs, was crucial for the enzymatic activity. | |||
Characterization of bacterial l-galactose dehydrogenase with l-glucose dehydrogenase activity from Luteolibacter sp. strain LG18.,Koubara K, Kim M, Takenoya M, Nakanishi A, Suzuki M, Azuma S, Ito S, Sasaki Y, Nakamura A, Yajima S Biosci Biotechnol Biochem. 2026 Mar 19:zbag041. doi: 10.1093/bbb/zbag041. PMID:41854348<ref>PMID:41854348</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9w7a" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Luteolibacter sp. LG18]] | ||
[[Category: Ito S]] | |||
[[Category: Koubara K]] | |||
[[Category: Nakamura A]] | |||
[[Category: Sasaki Y]] | |||
[[Category: Suzuki M]] | |||
[[Category: Takenoya M]] | |||
[[Category: Yajima S]] | |||
