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Purification, cryst...
Purification, crystallization and preliminary data analysis of FocB, a transcription factor regulating fimbrial adhesin expression in uropathogenic Escherichia coli
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- Wikström Hultdin, Ulrika (författare)
- Umeå universitet,Kemiska institutionen,Elisabeth Sauer-Eriksson
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- Lindberg, Stina, 1975- (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Bernt Eric Uhlin
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- Grundström, Christin (författare)
- Umeå universitet,Kemiska institutionen
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- Allgardsson, Anders (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Kemiska institutionen
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- Huang, Shenghua (författare)
- Umeå universitet,Kemiska institutionen
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- Stier, Günter (författare)
- Umeå universitet,Kemiska institutionen
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- Öhman, Anders (författare)
- Umeå universitet,Kemiska institutionen
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- Uhlin, Bernt Eric (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten)
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- Sauer-Eriksson, Elisabeth (författare)
- Umeå universitet,Kemiska institutionen
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(creator_code:org_t)
- 2010
- 2010
- Engelska.
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Ingår i: Acta Crystallographica. Section F. - 1744-3091 .- 1744-3091. ; 66:Pt 3, s. 337-341
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The transcription factor FocB belongs to a family of regulators encoded by several different fimbriae gene clusters in uropathogenic Escherichia coli. Recent findings suggest that FocB-family proteins may form different protein-protein complexes and that they may exert both positive and negative effects on the transcription of fimbriae genes. However, little is known about the actual role and mode of action when these proteins interact with the fimbriae operons. The 109-amino-acid FocB transcription factor from the foc gene cluster in E. coli strain J96 has been cloned, expressed and purified. The His6-tagged fusion protein was captured by Ni2+-affinity chromatography, cleaved with tobacco etch virus protease and purified by gel filtration. The purified protein is oligomeric, most likely in the form of dimers. NMR analysis guided the crystallization attempts by showing that probable conformational exchange or oligomerization is reduced at temperatures above 293 K and that removal of the highly flexible His6 tag is advantageous. The protein was crystallized using the hanging-drop vapour-diffusion method at 295 K. A native data set to 2.0 Å resolution was collected at 100 K using synchrotron radiation.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- fimbriae
- FocB
- transcription factors
- Chemistry
- Kemi
- biokemi
- Biochemistry
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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