View source for 4prl


==Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii==
<StructureSection load='4prl' size='340' side='right'caption='[[4prl]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4prl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_jensenii_1153 Lactobacillus jensenii 1153]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PRL 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=4prl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4prl OCA], [https://pdbe.org/4prl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4prl RCSB], [https://www.ebi.ac.uk/pdbsum/4prl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4prl ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The thermostable d-lactate dehydrogenase from Lactobacillus jensenii (Ljd-LDH) is a key enzyme in the production of the d-form of lactic acid from pyruvate concomitant with the oxidation of NADH to NAD(+). The polymers of d-lactic acid are used as biodegradable bioplastics. The crystal structures of Ljd-LDH and in complex with NAD(+) were determined at 2.13 and 2.60A resolutions, respectively. The Ljd-LDH monomer consists of the N-terminal substrate-binding domain and the C-terminal NAD-binding domain. The Ljd-LDH forms a homodimeric structure, and the C-terminal NAD-binding domain mostly enables the dimerization of the enzyme. The NAD cofactor is bound to the GxGxxG NAD-binding motif located between the two domains. Structural comparisons of Ljd-LDH with other d-LDHs reveal that Ljd-LDH has unique amino acid residues at the linker region, which indicates that the open-close dynamics of Ljd-LDH might be different from that of other d-LDHs. Moreover, thermostability experiments showed that the T50(10) value of Ljd-LDH (54.5 degrees C) was much higher than the commercially available d-lactate dehydrogenase (42.7 degrees C). In addition, Ljd-LDH has at least a 7 degrees C higher denaturation temperature compared to commercially available d-LDHs.

Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii.,Kim S, Gu SA, Kim YH, Kim KJ Int J Biol Macromol. 2014 Jul;68:151-7. doi: 10.1016/j.ijbiomac.2014.04.048. Epub, 2014 Apr 30. PMID:24794195<ref>PMID:24794195</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4prl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lactate dehydrogenase 3D structures|Lactate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactobacillus jensenii 1153]]
[[Category: Large Structures]]
[[Category: Kim KJ]]
[[Category: Kim S]]