001     32545
005     20200402210547.0
024 7 _ |2 DOI
|a 10.1016/j.jmb.2003.08.034
024 7 _ |2 WOS
|a WOS:000186102000001
037 _ _ |a PreJuSER-32545
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Menezes, R. A.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Sites for Interaction between Gal80p and Gal1p in Kluyveromyces latis: Structural Model of Galactokinase based on Homology to the GHMP Protein Family
260 _ _ |a Amsterdam [u.a.]
|b Elsevier
|c 2003
300 _ _ |a 479 - 492
336 7 _ |a Journal Article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a article
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440 _ 0 |a Journal of Molecular Biology
|x 0022-2836
|0 3552
|y 3
|v 333
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The induction of transcription of the galactose genes in yeast involves the galactose-dependent binding of ScGal3p (in Saccharomyces cerevisiae) or KlGal1p (in Kluyveromyces lactis) to Gal80p. This binding abrogates Gal80's inhibitory effect on the activation domain of Gal4p, which can then activate transcription. Here, we describe the isolation and characterization of new interaction mutants of K. lactis GAL1 and GAL80 using a two-hybrid screen. We present the first structural model for Gal1p to be based on the published crystal structures of other proteins belonging to the GHMP (galactokinase, homoserine kinase, mevalonate kinase and phosphomevalonate kinase) kinase family and our own X-ray diffraction data of Gal1p crystals at 3 Angstrom resolution.The locations of the various mutations in the modelled Gal1p structure identify domains involved in the interaction with Gal80p and provide a structural explanation for the phenotype of constitutive GAL1 mutations. (C) 2003 Elsevier Ltd. All rights reserved.
536 _ _ |a Neurowissenschaften
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588 _ _ |a Dataset connected to Web of Science
650 _ 7 |a J
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653 2 0 |2 Author
|a Kluyveromyces lactis
653 2 0 |2 Author
|a Gal1p-Gal80p interaction
653 2 0 |2 Author
|a protein interaction
653 2 0 |2 Author
|a Gal1p protein structure
653 2 0 |2 Author
|a galactose induction
700 1 _ |a Amuel, C.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Engels, R.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Gengenbacher, U.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Labahn, J.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB886
700 1 _ |a Hollenberg, E. M.
|b 5
|0 P:(DE-HGF)0
773 _ _ |a 10.1016/j.jmb.2003.08.034
|g Vol. 333, p. 479 - 492
|p 479 - 492
|q 333<479 - 492
|0 PERI:(DE-600)1355192-9
|t Journal of molecular biology
|v 333
|y 2003
|x 0022-2836
856 7 _ |u http://dx.doi.org/10.1016/j.jmb.2003.08.034
909 C O |o oai:juser.fz-juelich.de:32545
|p VDB
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2003
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
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980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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