%0 Journal Article
%A Graczer, E.
%A Konarev, P. V.
%A Szimler, T.
%A Bacso, A.
%A Bodonyi, A.
%A Svergun, D. I.
%A Zavodszky, P.
%A Vas, M.
%A DESY
%T Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase
%J FEBS letters
%V 585
%@ 0014-5793
%C Amsterdam [u.a.]
%I Elsevier
%M PHPPUBDB-23053
%P 3297-3302
%D 2011
%X X-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
%K 3-Isopropylmalate Dehydrogenase: chemistry
%K Bacterial Proteins: chemistry
%K Crystallography, X-Ray
%K Escherichia coli: enzymology
%K Metals: chemistry
%K Protein Structure, Tertiary
%K Thermus thermophilus: enzymology
%K Bacterial Proteins (NLM Chemicals)
%K Metals (NLM Chemicals)
%K 3-Isopropylmalate Dehydrogenase (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:21939659
%U <Go to ISI:>//WOS:000296514100023
%R 10.1016/j.febslet.2011.09.013
%U https://bib-pubdb1.desy.de/record/139261