View source for 8jsy


==Dihydrofolate reductase-like enzyme from Leptospira interrogans==
<StructureSection load='8jsy' size='340' side='right'caption='[[8jsy]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8jsy]] 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=8JSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JSY 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]] 2.55&#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=8jsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jsy OCA], [https://pdbe.org/8jsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jsy RCSB], [https://www.ebi.ac.uk/pdbsum/8jsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jsy 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 8jsy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptospira interrogans serovar Pomona]]
[[Category: Wangkanont K]]