1EZ4

CRYSTAL STRUCTURE OF NON-ALLOSTERIC L-LACTATE DEHYDROGENASE FROM LACTOBACILLUS PENTOSUS AT 2.3 ANGSTROM RESOLUTION

Summary for 1EZ4

• Entry DOI: 10.2210/pdb1ez4/pdb
• Descriptor: LACTATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: rossmann fold, oxidoreductase
• Biological source: Lactobacillus pentosus
• Cellular location: Cytoplasm (By similarity): P56511
• Total number of polymer chains: 4
• Total formula weight: 138803.58

Authors

Uchikoba, H.,Fushinobu, S.,Wakagi, T.,Konno, M.,Taguchi, H.,Matsuzawa, H. (deposition date: 2000-05-10, release date: 2001-12-28, Last modification date: 2024-02-07)

Primary citation

Uchikoba, H.,Fushinobu, S.,Wakagi, T.,Konno, M.,Taguchi, H.,Matsuzawa, H.
Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.
Proteins, 46:206-214, 2002

PubMed Abstract: L-Lactate dehydrogenase (LDH) from Lactobacillus pentosus is a non-allosteric enzyme, which shows, however, high sequence similarity to allosteric LDHs from certain bacteria. To elucidate the structural basis of the absence of allostery of L. pentosus LDH (LPLDH), we determined the crystal structure of LPLDH at 2.3 A resolution. Bacterial LDHs are tetrameric enzymes composed of identical subunits and exhibit 222 symmetry. The quaternary structure of LPLDH was similar to the active conformation of allosteric LDHs. Structural analysis revealed that the subunit interfaces of LPLDH are optimized mainly through hydrophilic interactions rather than hydrophobic interactions, compared with other LDHs. The subunit interfaces of LPLDH are more specifically stabilized by increased numbers of intersubunit salt bridges and hydrogen bonds, and higher geometrical complementarity. Such high specificity at the subunit interfaces should hinder the rearrangement of the quaternary structure needed for allosteric regulation and thus explain the "non-allostery" of LPLDH.

PubMed: 11807949
DOI: 10.1002/prot.1165

Experimental method

X-RAY DIFFRACTION (2.3 Å)