Literature summary for 1.1.1.85 extracted from

Graczer, E.; Merli, A.; Singh, R.K.; Karuppasamy, M.; Zavodszky, P.; Weiss, M.S.; Vas, M.
Atomic level description of the domain closure in a dimeric enzyme: Thermus thermophilus 3-isopropylmalate dehydrogenase (2011), Mol. Biosyst., 7, 1646-1659.

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-form without substrate and in complex with the divalent metalion, in complexes with both Mn2+ and 3-isopropylmalate, as well as with both Mn2+ and NADH, at resolutions ranging from 1.8 to 2.5 A. Identification of two hinges at the interdomain region, hinge 1 between alphad and betaF as well as hinge 2 between alphah and betaE with a possible operational mechanism upon the action of the substrates. The interactions of the protein with Mn2+ and isopropylmalate are mainly responsible for the domain closure. Upon binding into the cleft of the interdomain region, the substrate isopropylmalate induces a relative movement of the secondary structural elements betaE, betaF, betaG, alphad and alphah. A movement of the loop bearing the amino acid Tyr139 precedes the interacting arm of the subunit. The tyrosyl ring rotates and moves by at least 5 A upon substrate binding. Thereby, new hydrophobic interactions are formed above the buried isopropyl-group of isopropylmalate. Domain closure is then completed only through subunit interactions. A loop of one subunit that is inserted into the interdomain cavity of the other subunit extends the area with the hydrophobic interactions, providing an example of the cooperativity between interdomain and intersubunit interactions	Thermus thermophilus

Crystallization (Comment)

Organism

apo-form without substrate and in complex with the divalent metalion, in complexes with both Mn2+ and 3-isopropylmalate, as well as with both Mn2+ and NADH, at resolutions ranging from 1.8 to 2.5 A. Identification of two hinges at the interdomain region, hinge 1 between alphad and betaF as well as hinge 2 between alphah and betaE with a possible operational mechanism upon the action of the substrates. The interactions of the protein with Mn2+ and isopropylmalate are mainly responsible for the domain closure. Upon binding into the cleft of the interdomain region, the substrate isopropylmalate induces a relative movement of the secondary structural elements betaE, betaF, betaG, alphad and alphah. A movement of the loop bearing the amino acid Tyr139 precedes the interacting arm of the subunit. The tyrosyl ring rotates and moves by at least 5 A upon substrate binding. Thereby, new hydrophobic interactions are formed above the buried isopropyl-group of isopropylmalate. Domain closure is then completed only through subunit interactions. A loop of one subunit that is inserted into the interdomain cavity of the other subunit extends the area with the hydrophobic interactions, providing an example of the cooperativity between interdomain and intersubunit interactions

Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SIY4	-	-

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Release 2023.1 (January 2023)