Structural study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of two-dimensional crystals on a nickel-chelating lipid.
J Mol Biol
; 274(5): 687-92, 1997 Dec 19.
Article
em En
| MEDLINE
| ID: mdl-9405151
ABSTRACT
Two-dimensional crystals of the histidine-tagged-HupR protein, a transcriptional regulator from the photosynthetic bacterium Rhodobacter capsulatus, were obtained upon specific interaction with a Ni2+-chelated lipid monolayer. HupR is a response regulator of the NtrC family; it activates the transcription of the structural genes, hupSLC, of the [NiFe]hydrogenase. The lipid (Ni-NTA-DOGA) uses the metal chelator nitrilotriacetic group as the hydrophilic headgroup and contains unsaturated oleyl tails to provide the fluidity necessary for two-dimensional protein crystallization. A projection map of the full-length protein at 18 A resolution was generated by analysing electron microscopy micrographs of negatively stained crystals. The HupR protein appeared to be dimeric and revealed a characteristic "propeller-like" motif. Each monomer forms an L-shaped structure.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Fatores de Transcrição
/
Microscopia Eletrônica
/
Quelantes
/
Cristalografia
/
Proteínas de Ligação a DNA
/
Histidina
/
Lipídeos
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
França