1995
DOI: 10.1006/jmbi.1994.0103
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The Crystal Structure of Holo-glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic BacteriumThermotoga maritimaat 2.5 Å Resolution

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Cited by 227 publications
(182 citation statements)
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“…The observation that especially the subunit contacts are intensified by a strikin! ; increase in ion pairs (as found for the malate dehydrogenas,," from Thermusflavus [6] and the glutamate dehydrogenase fr~,m Pyrococcusfuriosus [5]) and hydrophobic interactions (as reported for the glyceraldehyde-3-phosphate dehydrogenase fr~,m Thermotoga maritima [4]) suggests that the subunit con-*(orresponding author. Fax: (49) (201) 183 2529.…”
Section: Introductionmentioning
confidence: 78%
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“…The observation that especially the subunit contacts are intensified by a strikin! ; increase in ion pairs (as found for the malate dehydrogenas,," from Thermusflavus [6] and the glutamate dehydrogenase fr~,m Pyrococcusfuriosus [5]) and hydrophobic interactions (as reported for the glyceraldehyde-3-phosphate dehydrogenase fr~,m Thermotoga maritima [4]) suggests that the subunit con-*(orresponding author. Fax: (49) (201) 183 2529.…”
Section: Introductionmentioning
confidence: 78%
“…From the suggested importance of the intersubunit contacts for thermostabilization, as deduced from experimental and comparative studies on various oligomeric enzymes [4][5][6][7], one should expect that the benefit of the higher association state resides in an increase of protein thermostability. The observation that the preference of a higher association state does not generally apply (or even countercurrent trends occur, as shown in the case of the enolases [25]) indicates that the advantage of association is limited by functional and/or structural restraints.…”
Section: Molecular Mass Determinationsmentioning
confidence: 99%
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“…For structure comparison, four GAPDH structures with resolutions higher than 2.5 A Ê in the Protein Data Bank were used. They are BS (entry 1GD1; Skarzynski et al, 1987), TM (entry 1HDG; Korndorfer et al, 1995), TA (entry 1CER; Tanner et al, 1996), and EC (entry 1GAD; Due  e et al, 1996). Of these, EC is mesophilic and the rest are thermophilic.…”
Section: Overall Structurementioning
confidence: 99%
“…GAPDH structures were ®rst determined for the enzymes from lobster (Homarus americanus) muscle, and then for that from the moderate thermophile Bacillus stearothermophilus in several conformational states (Moras et al, 1975;Murthy et al, 1980;Skarzynski et al, 1987;Skarzynski & Wonacott, 1988). In addition, there are several crystallographic investigations for enzymes from other species such as human muscle (Mercer et al, 1976), Bacillus coagulans (Grif®th et al, 1983), Trypanosoma brucei (Vellieux et al, 1993), Thermotoga maritima (Korndorfer et al, 1995), Thermus aquaticus (Tanner et al, 1996), and E. coli (Due  e et al, 1996). These structural investigations provide important information on the folding, catalysis, allosterism mechanism, as well as the thermal stability of this important enzyme.…”
Section: Introductionmentioning
confidence: 99%