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000139261 1001_ $$aGraczer, E.
000139261 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000139261 245__ $$aEssential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase
000139261 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2011
000139261 300__ $$a3297-3302
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000139261 440_0 $$0PERI:(DE-600)1460391-3$$aFEBS Letters$$v585$$x0014-5793$$y20
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000139261 520__ $$aX-ray structures of 3-isopropylmalate dehydrogenase (IPMDH) do not provide sufficient information on the role of the metal-ion in the metal-IPM assisted domain closure. Here solution studies were carried out to test its importance. Small-angle X-ray scattering (SAXS) experiments with the Thermus thermophilus enzyme (complexes with single substrates) have revealed only a very marginal (0-5%) extent of domain closure in the absence of the metal-ion. Only the metal-IPM complex, but neither the metal-ion nor the free IPM itself, is efficient in stabilizing the native protein conformation as confirmed by denaturation experiments with Escherichia coli IPMDH and by studies of the characteristic fluorescence resonance energy transfer (FRET) signal (from Trp to bound NADH) with both IPMDHs. A possible atomic level explanation of the metal-effect is given.
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000139261 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000139261 650_7 $$00$$2NLM Chemicals$$aMetals
000139261 650_7 $$0EC 1.1.1.85$$2NLM Chemicals$$a3-Isopropylmalate Dehydrogenase
000139261 650_2 $$2MeSH$$a3-Isopropylmalate Dehydrogenase: chemistry
000139261 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000139261 650_2 $$2MeSH$$aCrystallography, X-Ray
000139261 650_2 $$2MeSH$$aEscherichia coli: enzymology
000139261 650_2 $$2MeSH$$aMetals: chemistry
000139261 650_2 $$2MeSH$$aProtein Structure, Tertiary
000139261 650_2 $$2MeSH$$aThermus thermophilus: enzymology
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000139261 7001_ $$aKonarev, P. V.
000139261 7001_ $$aSzimler, T.
000139261 7001_ $$aBacso, A.
000139261 7001_ $$aBodonyi, A.
000139261 7001_ $$aSvergun, D. I.
000139261 7001_ $$aZavodszky, P.
000139261 7001_ $$aVas, M.
000139261 773__ $$0PERI:(DE-600)1460391-3$$a10.1016/j.febslet.2011.09.013$$gVol. 585, p. 3297-3302$$p3297-3302$$q585<3297-3302$$tFEBS letters$$v585$$x0014-5793$$y2011
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