4prl: Difference between revisions
New page: '''Unreleased structure''' The entry 4prl is ON HOLD Authors: Kim, S., Kim, K.-J. Description: Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==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=''> | |||
== 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]] 2.6Å</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®/PubMed®, 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]] | |||
Latest revision as of 18:00, 8 November 2023
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. See AlsoReferences
|
| ||||||||||||||||||