4PRL

Crystal structure of D-lactate dehydrogenase with NAD+ from Lactobacillus jensenii

Summary for 4PRL

• Entry DOI: 10.2210/pdb4prl/pdb
• Related: 4PRK
• Descriptor: 4-phosphoerythronate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase, rossmann fold, nad
• Biological source: Lactobacillus jensenii
• Total number of polymer chains: 2
• Total formula weight: 75527.78

Authors

Kim, S.,Kim, K.J. (deposition date: 2014-03-06, release date: 2014-06-18, Last modification date: 2023-11-08)

Primary citation

Kim, S.,Gu, S.A.,Kim, Y.H.,Kim, K.J.
Crystal structure and thermodynamic properties of d-lactate dehydrogenase from Lactobacillus jensenii.
Int.J.Biol.Macromol., 68C:151-157, 2014

PubMed Abstract: 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 2.60Å 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°C) was much higher than the commercially available d-lactate dehydrogenase (42.7°C). In addition, Ljd-LDH has at least a 7°C higher denaturation temperature compared to commercially available d-LDHs.

PubMed: 24794195
DOI: 10.1016/j.ijbiomac.2014.04.048

Experimental method

X-RAY DIFFRACTION (2.6 Å)