View source for 8jt0


==Dihydrofolate reductase-like enzyme from Leptospira interrogans with additional NADP+==
<StructureSection load='8jt0' size='340' side='right'caption='[[8jt0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8jt0]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_interrogans_serovar_Pomona Leptospira interrogans serovar Pomona]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JT0 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=8jt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jt0 OCA], [https://pdbe.org/8jt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jt0 RCSB], [https://www.ebi.ac.uk/pdbsum/8jt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jt0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0AA40WBR8_LEPIR A0AA40WBR8_LEPIR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A dihydrofolate reductase (DHFR)-like enzyme from Leptospira interrogans (LiDHFRL) was cloned and the recombinant protein was characterized. Sequence alignment suggested that the enzyme lacked the conserved catalytic residues found in DHFR. Indeed, LiDHFRL did not catalyze the reduction of dihydrofolate by either NADH or NADPH. X-ray crystallography revealed that LiDHFRL bound NADP(H) tightly, but its active site architecture was vastly different from that of Escherichia coli DHFR (EcDHFR) and other DHFRLs. Interestingly, vanillin could serve as a substrate for LiDHFRL, demonstrating that LiDHFRL is a functional enzyme. A putative vanillin binding mode was proposed.

Structure and catalytic activity of a dihydrofolate reductase-like enzyme from Leptospira interrogans.,Chandit C, Hengphasatporn K, Donsuy P, Shigeta Y, Wangkanont K Int J Biol Macromol. 2025 Jan 15;298:139931. doi: 10.1016/j.ijbiomac.2025.139931. PMID:39824401<ref>PMID:39824401</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8jt0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptospira interrogans serovar Pomona]]
[[Category: Wangkanont K]]