Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase

Buehner, Manfred; Ford, Geoffrey C.; Moras, Dino; Olsen, Kenneth W.; Rossmann, Michael G.

doi:10.1016/0022-2836(74)90254-x

Cited by 252 publications

(41 citation statements)

References 76 publications

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“…Maximum absorption is at about 360 nm and used by most researchers, particularly in assessing NAD + binding. The Racker band is produced by the charge transfer complex between Cys-149 and the nicotinamide ring of NAD + [20]. The close proximity of Tyr-317 may also be contributing to this electronic absorption band.…”

Section: Cooperativitymentioning

confidence: 98%

Dynamic Oligomeric Properties

Seidler

2012

GAPDH: Biological Properties and Diversity

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This chapter provides a foundation for further research into the relationship between dynamic oligomeric properties and functional diversity. The structural basis that underlies the conformational sub-states of the GAPDH oligomer is discussed. The issue of protein stability is given a thorough analysis, since it is well-established that the primary strategy for protein oligomerization is to stabilize conformation. Several factors that affect oligomerization are described, including chemical modification by synthetic reagents. The effects of native substrates and coenzymes are also discussed. The curious feature of chloride ions having a de-stabilizing effect on native GAPDH structure is described. Additionally, the role of adenine dinucleotides in tetramer-dimer equilibrium dynamics is suggested to be a major part of the physiological regulation of GAPDH structure and function. This chapter also contends that a vast amount of useful information can come from comparative analyses of diverse species, particularly regarding protein stability and subunit-subunit interaction. Lastly, the concept of domain exchange is introduced as a means of understanding the stabilization of dynamic oligomers, suggesting that inter-subunit contacts may also be a way of masking docking sites to other proteins.

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Section: Cooperativitymentioning

confidence: 98%

Dynamic Oligomeric Properties

Seidler

2012

GAPDH: Biological Properties and Diversity

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“…The nucleotide lies across the end of a fl-pleated sheet, and its c~-phosphate is thought to interact with the positive dipole at the N-terminal end of the a-helix (Hol et al, 1978). In specific cases other residues are also involved in binding the nucleotide; for example, aspartate residues may interact with the Mg ~-+ of nucleoside triphosphates (Jurnak, 1985), form hydrogen bonds to the 2' hydroxyl group of the ribose (Buehner et al, 1974) or interact with the amino group of the purine ring (Jurnak, 1985). It is the different strategies by which distinct classes of nucleotide-binding protein hold the nucleotide (often also different) on the common fief-loop that makes the positioning of conserved residues in the primary structure diagnostic for a class of protein.…”

Section: Structural Aspects Of Protein Kinasesmentioning

confidence: 99%

Viral Aspects of Protein Phosphorylation

Leader

Katan

1988

Journal of General Virology

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“…For instance, the phosphoryl-binding loop of lobster glyceraldehyde-3-phosphate dehydrogenase, located near the amino terminus of the protein, follows the dinucleotide consensus sequence 4GIDGFGRIGR13 [50,51] with the exception of the second hydrophobic residue, which is replaced by an aspartic acid residue. Other examples of dinucleotide proteins in which the consensus sequence has not been found are mercuric reductase and yeast alcohol dehydrogenase (table 2).…”

Section: Sequences In Dinucleotide-binding Proteinsmentioning

confidence: 99%

Phosphate‐binding sequences in nucleotide‐binding proteins

Möller¹,

Amons²

1985

FEBS Letters

300

137

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In the three-dimensional model of adenylate kinase, the phosphate-binding site for AMP and ATP has been identified [Pai, E.F. et al. (1977) J. Mol. Biol. 114, 37451. In this region one can distinguish a sequence glycine XXXX glycinelysine. The same sequence is found in many other mononucleotide-binding proteins including elongation factors and oncogenic P2 I proteins. Dinucleotide-binding proteins display a pyrophosphate-binding unit with a glycine pattern different from that of mononucleotide-binding proteins. It has been found that P2l ras protein possesses a strand motif typical for (pyro)phosphate binding of a mononucleotide. A single mutation at position 12 can confer oncogenic activity on the protein. Based on the assumption that amino acid residues which are critical for function are preferentially conserved, we predict from the sequence that glycine residue I5 rather than residue I2 is important for (pyro)phosphate binding.

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Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase

Cited by 252 publications

References 76 publications

Dynamic Oligomeric Properties

Dynamic Oligomeric Properties

Viral Aspects of Protein Phosphorylation

Phosphate‐binding sequences in nucleotide‐binding proteins

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