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Two crystal forms of ModE, the molybdate-dependent transcriptional regulator from Escherichia coli.
Hall, D R; Gourley, D G; Duke, E M; Leonard, G A; Anderson, L A; Pau, R N; Boxer, D H; Hunter, W N.
Affiliation
  • Hall DR; The Wellcome Trust Building, Department of Biochemistry, University of Dundee, Dundee DD1 5EH, Scotland.
Acta Crystallogr D Biol Crystallogr ; 55(Pt 2): 542-3, 1999 Feb.
Article in En | MEDLINE | ID: mdl-10089372
The molybdenum-responsive ModE regulatory protein from Escherichia coli has been purified and used in crystallization trials. Two crystal forms have been observed. Form I is tetragonal, P41212 (or enantiomorph), with a = b = 72.3, c = 246.2 A and diffracts to medium resolution. Form II is orthorhombic, P21212, with a = 82.8, b = 127.9, c = 64.0 A and diffraction has been observed beyond 2.8 A resolution. Structural analysis, in combination with ongoing biochemical characterization, will assist the elucidation of the structure-activity relationship in regulating the uptake of molybdate in bacteria.
Subject(s)
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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Transcription Factors / Escherichia coli Proteins Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 1999 Document type: Article Affiliation country: Country of publication:
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Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Transcription Factors / Escherichia coli Proteins Language: En Journal: Acta Crystallogr D Biol Crystallogr Year: 1999 Document type: Article Affiliation country: Country of publication: