Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase

Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase of, 2, 4, 9, 22 apoenzyme, 19... 

Comparative studies on proteins from different species show that the structures are essentially the same despite different crystallisation conditions. Examples include sperm whale and seal myoglobin, horse and human haemoglobin, horse, tuna, bonito and rice cytochrome c, hen egg white, tortoise egg white and human lysozyme, horse and yeast phosphoglycerate kinase, porcine and hagfish insulin and lobster and Bacillus stearothermophilus glyceraldehyde 3-phosphate dehydrogenase. Coordinates for these proteins are held in the Protein Data Bank [151]. 

Fig. 2.35. Schematic diagram of the structure of Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase (according to Biesecker et aL, 1977 courtesy of J. Walker) The first domain, NAD binding domain, consists of residues 1-149 organized in two Ross-mann folds the position of NAD is indicated. In the second domain (residues 150-311), an extensive region of antiparallel p sheet form a subunit interface the S loop is formed by residues 178-201 the C-terminal helix (residues 312-333) fits into a groove in the first domain.

Figure 2-13 (A) Stereoscopic view of the nucleotide binding domain of glyceraldehyde phosphate dehydrogenase. The enzyme is from Bacillus stearothermophilus but is homologous to the enzyme from animal sources. Residues are numbered 0-148. In this wire model all of the main chain C, O, and N atoms are shown but side chains have been omitted. The large central twisted P sheet, with strands roughly perpendicular to the page, is seen clearly hydrogen bonds are indicated by dashed lines. Helices are visible on both sides of the sheet. The coenzyme NAD+ is bound at the end of the P sheet toward the viewer. Note that the two phosphate groups in the center of the NAD+ are H-bonded to the N terminus of the helix beginning with RIO. From Skarzynski et al.llla (B) Structural formula for NAD+.

Figure 16.1 The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. [From G. Biesecker, J. I. Harris, J. C. Thierry, J. E. Walker, and A. J. Wonacott, Nature, Lond. 266, 328 (1977).]...

Skarzynski, T., Moody, P. C., and Wonacott, A. J., 1987. Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. J. Mol. Biol. 193 171-187. 

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