Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond.
Isupov
M N
MN
Schools of Chemistry and Biological Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.
Fleming
T M
TM
Dalby
A R
AR
Crowhurst
G S
GS
Bourne
P C
PC
Littlechild
J A
JA
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology / Q000235:genetics; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D016944:Sulfolobus / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
D011994:Recombinant Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases