Projection structure of a transcriptional regulator, HupR, determined by electron cryo-microscopy
Identifieur interne : 003995 ( Main/Curation ); précédent : 003994; suivant : 003996Projection structure of a transcriptional regulator, HupR, determined by electron cryo-microscopy
Auteurs : Catherine Vénien-Bryan [Royaume-Uni] ; Gebhard F. X Schertler [Royaume-Uni] ; Eric Thouvenin ; Sébastien CourtySource :
- Journal of Molecular Biology [ 0022-2836 ] ; 2000.
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Abstract
Large, well-ordered two-dimensional crystals of the histidine-tagged-HupR protein, a transcriptional regulator from the photosynthetic bacterium Rhodobacter capsulatus, were obtained by specific interaction with a Ni2+-chelated lipid monolayer. HupR is a response regulator of the NtrC subfamily; it activates the transcription of the structural genes hupSLC, of [NiFe]hydrogenase. A projection map of the full-length protein at 9 Å resolution was obtained by electron cryo-microscopy and image analysis of frozen-hydrated two-dimensional crystals. The crystals have a p6 plane group with unit cell dimensions of a = b = 111.6(±1.0) Å, γ = 120.4(±0.5)°. The structure of the N-terminal domain of NtrC, the family to which HupR belongs, had been determined previously by NMR. The atomic coordinates of the N-terminal domain of NtrC, were compared to the structure obtained by cryo-electron microscope techniques of the whole HupR. These results provide the first structure at medium resolution of a whole transcription factor, HupR from the NtrC family.
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DOI: 10.1006/jmbi.1999.3480
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Eric Thouvenin<affiliation><wicri:noCountry code="no comma">Institut de Biologie Structurale Jean-Pierre Ebel (CEA-CNRS) 41 rue Jules Horowitz 38027 Grenoble cedex 1 France</wicri:noCountry></affiliation><affiliation><wicri:noCountry code="no comma">Institut de Biologie Structurale Jean-Pierre Ebel (CEA-CNRS) 41 rue Jules Horowitz 38027 Grenoble cedex 1 France</wicri:noCountry></affiliation>Le document en format XML
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