Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase

Moras, Dino; Olsen, KW; Sabesan, M.N.; Buehner, Manfred; Ford, GC; Rossmann, M.G.

doi:10.1016/s0021-9258(19)40703-5

Cited by 313 publications

(116 citation statements)

References 60 publications

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“…Since sulphate ions, a component of the crystal suspending medium, strongly inhibit enzyme activity, diffusion was expected to be comparatively fast with respect to chemical reactions. Most of our spectroscopic studies were carried out using monoclinic crystals of the enzyme from the tail muscle of the Mediterranean lobster Palinurus vulgaris but qualitatively similar results were obtained using crystals of the enzyme from the tail muscle of Homarus americanus, the structure of which had been determined (Moras et al 1975).…”

Section: (B)mentioning

confidence: 63%

“…Mozzarelli, unpublished results). The three-dimensional structure of this enzyme has been determined (Biesecker et al 1977) and the active site geometry appears to be very similar to th a t of the muscle enzyme (Moras et al 1975). Therefore, the intriguing structural basis of negative cooperativity of the muscle enzyme might turn out to be hard to detect.…”

Section: Discussionmentioning

confidence: 97%

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Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Rossi

Mozzarelli

Peracchi

et al. 1992

Phil. Trans. R. Soc. Lond. A

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The functional properties of proteins in the crystalline state have been investigated over the past 30 years by a variety of methods, including single crystal polarized absorption spectroscopy. This technique has provided information on the accumulation and equilibrium distribution of protein-ligand complexes in the crystal and, in a few cases, on the rates of interconversion of catalytic intermediates. It has been possible to detect synergistic effects in the binding of different ligands, cooperativity and half-site reactivity and even formation of active multiprotein complexes, obtained by diffusion of one small protein in the pre-formed crystals of the other. Lattice interactions restrain the conformational transitions of some proteins existing in multiple states in solution. The crystal offers the unique opportunity to analyse not only the structure but also the function of a single form of the protein. The relevance of these data to the planning and interpretation of structural studies, especially in the perspectives of time-resolved crystallography, will be discussed with reference to well-characterized systems.

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Section: (B)mentioning

confidence: 63%

Section: Discussionmentioning

confidence: 97%

Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Rossi

Mozzarelli

Peracchi

et al. 1992

Phil. Trans. R. Soc. Lond. A

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“…The subunit of the enzyme is composed of two domains; the coenzyme-binding domain closely resembles those of lactate and alcohol dehydrogenases (Rossmann al. 1975).…”

Section: Structure O F Glyceraldehyde-3-phosphate Dehydrogenasementioning

confidence: 99%

“…The active site is in a cleft between the coenzyme-binding domain and the catalytic domain, with the essential thiol group of Cys 149 close to the nicotinamide C-4 atom of NAD+ (figure 6). The unique feature of this enzyme is an S-shaped loop in the catalytic domain comprising residues 178-201 (Moras et al 1975;Biesecker et al 1977).…”

Section: Structure O F Glyceraldehyde-3-phosphate Dehydrogenasementioning

confidence: 99%

“…High resolution structures have been computed for the crystalline enzyme from lobster tail muscle (Buehner al. 1974;Moras et al 1975) and Bacillus stearothermophilus (Biesecker et al 1977). Complete amino acid sequences were established for the enzymes from these sources and from pig muscle, yeast and Thermus aquaticus by Harris and his coworkers.…”

Section: Introductionmentioning

confidence: 99%

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Glyceraldehyde-3-phosphate dehydrogenase

Dalziel

McFerran

Wonacott

1981

Phil. Trans. R. Soc. Lond. B

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Conflicting experimental evidence of the pathway of catalysis for the enzyme from rabbit, pig and lobster muscle tissues is reviewed. Transient kinetic studies with the enzyme from rabbit muscle are presented. The results are shown to be consistent with the double-displacement mechanism of catalysis originally proposed by Segal & Boyer (1953). The rate constant for combination of the aldehyde form of the substrate with the NAD+ complex of the enzyme is about 3 X 10(7) M-1 S-1, and for all four subunits of the molecule the rate constant for hydride transfer in the ternary complex formed is greater than 10(3) S-1, consistent with their simultaneous participation in catalysis. Recent steady-state kinetic studies with the rabbit muscle enzyme, in contrast to earlier studies, also provide evidence to support the Segal-Boyer pathway if the kinetic effects of the negative cooperativity of NAD+ binding are taken into account. Experimental data for the binding of NAD+ to the enzyme from muscles and from Bacillus stearothermophilus, and their interpretations, are also briefly reviewed. The information currently available from X-ray crystallography regarding the structures of holoenzyme and apoenzyme from B. stearothermophilus and lobster muscle is outlined.

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Overview of Protein Structural and Functional Folds

2004

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This overview provides an illustrated, comprehensive survey of some commonly observed protein-fold families and structural motifs, chosen for their functional significance. It opens with descriptions and definitions of the various elements of protein structure and associated terminology. Following is an introduction into web-based structural bioinformatics that includes surveys of interactive web servers for protein fold or domain annotation, protein-structure databases, protein-structure-classification databases, structural alignments of proteins, and molecular graphics programs available for personal computers. The rest of the overview describes selected families of protein folds in terms of their secondary, tertiary, and quaternary structural arrangements, including ribbon-diagram examples, tables of representative structures with references, and brief explanations pointing out their respective biological and functional significance.

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Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase

Cited by 313 publications

References 60 publications

Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Time course of chemical and structural events in protein crystals measured by microspectrophotometry

Glyceraldehyde-3-phosphate dehydrogenase

Overview of Protein Structural and Functional Folds

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