TY  - JOUR
AU  - Graczer, E.
AU  - Konarev, P. V.
AU  - Szimler, T.
AU  - Bacso, A.
AU  - Bodonyi, A.
AU  - Svergun, D. I.
AU  - Zavodszky, P.
AU  - Vas, M.
AU  - DESY
TI  - Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase
JO  - FEBS letters
VL  - 585
SN  - 0014-5793
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PHPPUBDB-23053
SP  - 3297-3302
PY  - 2011
AB  - 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
KW  - 3-Isopropylmalate Dehydrogenase: chemistry
KW  - Bacterial Proteins: chemistry
KW  - Crystallography, X-Ray
KW  - Escherichia coli: enzymology
KW  - Metals: chemistry
KW  - Protein Structure, Tertiary
KW  - Thermus thermophilus: enzymology
KW  - Bacterial Proteins (NLM Chemicals)
KW  - Metals (NLM Chemicals)
KW  - 3-Isopropylmalate Dehydrogenase (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:21939659
UR  - <Go to ISI:>//WOS:000296514100023
DO  - DOI:10.1016/j.febslet.2011.09.013
UR  - https://bib-pubdb1.desy.de/record/139261
ER  -