A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes

White, Janice L.; Hackert, Marvin L.; Buehner, Manfred; Adams, Margaret; Ford, Geoffrey C.; Lentz, P. J.; Smiley, Ira E.; Steindel, Steven J.; Rossmann, Michael G.

doi:10.1016/0022-2836(76)90290-4

Cited by 183 publications

(35 citation statements)

References 21 publications

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“…Structural analyses of LDH from a range of species are well advanced and include crystal structures of these enzymes from dogfish, 3 pig, 4,5 Bacillus stearothermophilus, 6 Bifidobacterium longum,, 7 and Plasmodium falciparum. 8 Despite considerable amino acid sequence diversity between each of these proteins, a high level of structural similarity is preserved.…”

Section: Introductionmentioning

confidence: 99%

Structural basis for altered activity of M‐ and H‐isozyme forms of human lactate dehydrogenase

Winter²,

et al. 2001

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Section: Introductionmentioning

confidence: 99%

Structural basis for altered activity of M‐ and H‐isozyme forms of human lactate dehydrogenase

Winter²,

et al. 2001

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“…In dogfish lactate dehydrogenase the NAD binding motif, babab fold, is a continuous 60 residues long segment (PDB ID: 3LDH) [4]. In contrast, in yeast D-amino acid oxidase, the FAD binding domain includes only the initial bab fold in a continuous segment of 30 residues, but between the second and third b-strands there is long stretch of 121 residues that includes four helical segments and three b-strands located in a different region of the enzyme (PDB ID: 1C0I) [5].…”

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confidence: 99%

Proteopedia: Rossmann fold: A beta‐alpha‐beta fold at dinucleotide binding sites

Hanukoglu

2015

Biochem Molecular Bio Educ

117

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The Rossmann fold is one of the most common and widely distributed super-secondary structures. It is composed of a series of alternating beta strand (b) and alpha helical (a) segments wherein the b-strands are hydrogen bonded forming a b-sheet. The initial beta-alpha-beta (bab) fold is the most conserved segment of Rossmann folds. As this segment is in contact with the ADP portion of dinucleotides such as FAD, NAD, and NADP it is also called as an "ADPbinding bab fold". The Proteopedia entry on the Rossmann fold (Available at: http://proteopedia.org/w/Rossmann_fold) was generated to illustrate several structural aspects of super families of FAD and NAD(P) binding proteins: (1) The coenzymes FAD and NAD(P) share the basic adenosine diphosphate (ADP) structure. (2) The bab fold motif that is common to both FAD and NAD(P) binding enzymes accommodates the common ADP component of these two coenzymes. (3) In both FAD and NAD(P) binding sites, the tight turn between the first b-strand and the a-helix is in contact with the two phosphate groups of ADP. (4) Keywords: protein structure function and folding; enzymes and catalysis; protein design; biochemical evolution; molecular graphics and representations; comparative biochemistryIn a very large superfamily of dinucleotide binding enzymes, the domains that bind a dinucleotide such as FAD, NAD, and NADP share a common super-secondary structure that is partly composed of a series of alternating beta strand (b) and alpha helical (a) segments wherein the b-strands are hydrogen bonded forming a central b-sheet with helices on either side. There can be up seven strands in one sheet. This domain structure was named "Rossmann fold" after Michael G. Rossmann who first reported it as a common structure in a variety of nucleotide binding proteins, such as lactate dehydrogenase and flavodoxin [1].The Rossmann fold is one of the five most common structural motifs that appear in a myriad of proteins [2,3]. The most widely distributed protein folding motifs are thought to be remnants of most ancient protein architectures [2,3]. In many textbooks, the Rossmann fold is defined as a babab structure in accordance with the original report [1]. However, elucidation of the structures of many dinucleotide binding enzymes revealed a great diversity in the overall structure of the dinucleotide binding domains. The major differences among dinucleotide binding domains of proteins include extensive divergence of the primary structure, variable number of b-strands in the complete b-sheet that forms the Rossmann fold, and large variations in the length and secondary structure of the segment that connects the second and third b-strands.The diversity of the Rossmann fold can be illustrated by two enzymes as examples. In dogfish lactate dehydrogenase the NAD binding motif, babab fold, is a continuous 60 residues long segment (PDB ID: 3LDH) [4]. In contrast, in yeast D-amino acid oxidase, the FAD binding domain includes only the initial bab fold in a continuous segment of 30 residues, but betwee...

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“…Then, the protein solution was removed from file SPR cuvette, and the surfaces were washed with clean buffer solution and with the same buffer solution containing 0.5 mM NADH (Sigma). The remaining enzy-matic surface coverages were calculated assuming that a densely packed LDH-monolayer gives rise to a protein layer thickness of 11.6 nm (theoretical value calculated assuming that each LDH subunit is a sphere with an approximated radius of 58 ,A [35], and that the whole LDH tetramer lays flat on the monolayer facing all subunits to the metal surface).…”

Section: Enzymatic Complexes: Estimation Of Surface Coveragesmentioning

confidence: 99%

Self-assembled monolayers with biospecific affinity for lactate dehydrogenase for the electroenzymatic oxidation of lactate

Schlereth

Kooyman

1997

Journal of Electroanalytical Chemistry

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Surface modified gold electrodes with high biospecific affinity for NAD(H)-dependent lactate dehydrogenase have been prepared by covalent attachment of several triazine dyes to stepwise functionalized mixed alkanethiol self-assembled monolayers. The biospecific affinity of such ligand-anchored monolayers to bind submonolayer amounts of enzyme was demonstrated from the course of the protein adsorption events monitored by surface plasmon resonance. Electr~nzymatic activity measurements of lactate dehydrogenase modified surfaces for the reaction of lactate oxidation, carded out 'ex situ' at different stages of protein layer growth, allowed the optimization of the preparative procedure to yield reproducible enzymatic electrodes with a low amount of unspecifically bound protein. A short adsorption time, as well as a high concentration of enzyme in the solution used for protein layer growth, led to lactate dehydrogenasemodified gold electrode surfaces with a high electroenzymatic activity arising mainly from biospecifically bound species. The lowest amount of unspecifically adsorbed protein was found for ligand-anchored monolayers prepared fi'om mixed alkanethiol underlayers with an excess of positively charged groups. The lack of electroenzymatic activity shown by lactate dehydrogenase modified electrodes in the absence of soluble coenzyme (NAD +) indicates that none of the investigated ligand-anchored monolayers could provide an efficient electronic pathway from the metal to the active site of the enzyme. Therefore, the monolayers acted just as an anchoring system for lactate dehydrogenase. © 1997 Elsevier Science S.A.

show abstract

A comparison of the structures of apo dogfish M4 lactate dehydrogenase and its ternary complexes

Cited by 183 publications

References 21 publications

Structural basis for altered activity of M‐ and H‐isozyme forms of human lactate dehydrogenase

Structural basis for altered activity of M‐ and H‐isozyme forms of human lactate dehydrogenase

Proteopedia: Rossmann fold: A beta‐alpha‐beta fold at dinucleotide binding sites

Self-assembled monolayers with biospecific affinity for lactate dehydrogenase for the electroenzymatic oxidation of lactate

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