4prl: Difference between revisions
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==Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii== | ==Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii== | ||
<StructureSection load='4prl' size='340' side='right' caption='[[4prl]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='4prl' size='340' side='right' caption='[[4prl]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4prk|4prk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4prk|4prk]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-phosphoerythronate_dehydrogenase 4-phosphoerythronate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.290 1.1.1.290] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-phosphoerythronate_dehydrogenase 4-phosphoerythronate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.290 1.1.1.290] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4prl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4prl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4prl RCSB], [http://www.ebi.ac.uk/pdbsum/4prl PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4prl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4prl OCA], [http://pdbe.org/4prl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4prl RCSB], [http://www.ebi.ac.uk/pdbsum/4prl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4prl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4prl" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:20, 11 August 2016
Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jenseniiCrystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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