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| 001 | 139261 | ||
| 005 | 20250730164212.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21939659 |
| 024 | 7 | _ | |2 ISSN |a 1873-3468 |
| 024 | 7 | _ | |2 ISSN |a 0014-5793 |
| 024 | 7 | _ | |2 doi |a 10.1016/j.febslet.2011.09.013 |
| 024 | 7 | _ | |2 WOS |a WOS:000296514100023 |
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| 037 | _ | _ | |a PHPPUBDB-23053 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Graczer, E. |
| 110 | 1 | _ | |a DESY |b European Molecular Biology Laboratory |
| 245 | _ | _ | |a Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2011 |
| 300 | _ | _ | |a 3297-3302 |
| 336 | 7 | _ | |0 0 |2 EndNote |a Journal Article |
| 336 | 7 | _ | |2 DRIVER |a article |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |b journal |m journal |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
| 440 | _ | 0 | |0 PERI:(DE-600)1460391-3 |a FEBS Letters |v 585 |x 0014-5793 |y 20 |
| 500 | _ | _ | |3 Converted on 2013-05-30 09:24 |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:21 |
| 520 | _ | _ | |a 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%) 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. |
| 536 | _ | _ | |0 G:(DE-H253)POF2-D1.2-20130405 |f POF II |x 0 |c POF2-54G13 |a DORIS Beamline D1.2 (POF2-54G13) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Bacterial Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Metals |
| 650 | _ | 7 | |0 EC 1.1.1.85 |2 NLM Chemicals |a 3-Isopropylmalate Dehydrogenase |
| 650 | _ | 2 | |2 MeSH |a 3-Isopropylmalate Dehydrogenase: chemistry |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Escherichia coli: enzymology |
| 650 | _ | 2 | |2 MeSH |a Metals: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Thermus thermophilus: enzymology |
| 693 | _ | _ | |0 EXP:(DE-H253)D-D1.2-20150101 |1 EXP:(DE-H253)DORISIII-20150101 |6 EXP:(DE-H253)D-D1.2-20150101 |a DORIS III |f DORIS Beamline D1.2 |x 0 |
| 700 | 1 | _ | |a Konarev, P. V. |
| 700 | 1 | _ | |a Szimler, T. |
| 700 | 1 | _ | |a Bacso, A. |
| 700 | 1 | _ | |a Bodonyi, A. |
| 700 | 1 | _ | |a Svergun, D. I. |
| 700 | 1 | _ | |a Zavodszky, P. |
| 700 | 1 | _ | |a Vas, M. |
| 773 | _ | _ | |0 PERI:(DE-600)1460391-3 |a 10.1016/j.febslet.2011.09.013 |g Vol. 585, p. 3297-3302 |p 3297-3302 |q 585<3297-3302 |t FEBS letters |v 585 |x 0014-5793 |y 2011 |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/139261/files/Graszer_2011.pdf |y OpenAccess |
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| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/139261/files/Graszer_2011.jpg?subformat=icon-640 |x icon-640 |y OpenAccess |
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| 910 | 1 | _ | |0 I:(DE-588b)2008985-5 |a Deutsches Elektronen-Synchrotron |k DESY |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |a Externes Institut |k Extern |
| 913 | 2 | _ | |0 G:(DE-HGF)POF3-621 |1 G:(DE-HGF)POF3-620 |2 G:(DE-HGF)POF3-600 |9 G:(DE-HGF)POF3-6215 |a DE-HGF |b Forschungsbereich Materie |l Von Materie zu Materialien und Leben |v In-house research on the structure, dynamics and function of matter |x 0 |
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| 914 | 1 | _ | |a (c) Elsevier B.V. |y 2011 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |2 StatID |a JCR/ISI refereed |
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