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The crystal structure of holo-GAPDH from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
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94. Korndörfer I, Steipe B, Huber R, Tomschy A, Jaenicke R: The crystal structure of holo-GAPDH from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J Mol Biol 1995, 246:512-521.
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95
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0028994307
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2.0 Å structure of indole-3-glycerol phosphate dehydrogenase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
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95. Hennig M, Darimont B, Sterner R, Kirschner K, Jansonius JN: 2.0 Å structure of indole-3-glycerol phosphate dehydrogenase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure 1995, 3:1295-1306.
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Hennig, M.1
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96
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0031567156
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Crystal structures of E. Coli and S. Typhimurium 3-isopropyl MDH and comparison with their thermophilic counterpart from Thermus thermophilus
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96. Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA: Crystal structures of E. coli and S. typhimurium 3-isopropyl MDH and comparison with their thermophilic counterpart from Thermus thermophilus. J Mol Biol 1997, 266:1016-1031. All three 3-isopropyl malate dehydrogenase (IPMDH) structures show a resolution < 2.1 Å. The main stabilizing features in thermophilic IPMDH are an increased number of ion pairs, additional hydrogen bonds, a proportionately larger and more hydrophobic subunit interface, shortened N and C termini, and a larger number of proline residues. Aromatic-aromatic interactions, helical capping and cavities seem to be of lesser importance. The overall flexibility (monitored by the B factors of equivalent residues) is reduced in the case of S. typhimurium IPMDH.
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J Mol Biol
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Wallon, G.1
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97
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Serial increase in the thermal stability of IPMDH from Bacillus subtilis by experimental evolution
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97. Akanuma S, Yamagishi A, Tanaka N, Oshima T: Serial increase in the thermal stability of IPMDH from Bacillus subtilis by experimental evolution. Protein Sci 1998, 7:678-705. The mesophilic IPMDH from B. subtilis was expressed in an IPMDH-deficient mutant of T. thermophilus. Variants growing at temperatures higher than the stability limit of wildtype B. subtilis IPMDH (56°C) were selected at 61-70°C. Three point mutants, I95L, M292I and T308I, and double and triple mutants thereof were isolated and characterized: The stability of the variants was improved, showing additivity in their stabilization effects, and the triple mutant had also higher specific activity than the wildtype protein.
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(1998)
Protein Sci
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Akanuma, S.1
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98
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Stabilization of E. Coli IPMDH by single amino acid substitutions
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98. Aoshima M, Oshima T: Stabilization of E. coli IPMDH by single amino acid substitutions. Protein Eng 1997, 10:249-254. In attempting to define the key positions responsible for the high stability of IPMDH from Thermus thermophilus (Tt) and Thermus aquaticus (Ta), sequence comparisons of all 20 known IPMDHs were carried out. As a result, a four-residue motif, which is present in the Tt and Ta sequences only, was found located between two highly conserved stretches of the sequence. Introducing this motif into E. coli IPMDH, one by one, enhanced thermostability, whereas introducing the whole motif caused destabilization. The three-dimensional structure allows a tentative explanation of the mechanism.
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(1997)
Protein Eng
, vol.10
, pp. 249-254
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Aoshima, M.1
Oshima, T.2
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