1UXC

FRUCTOSE REPRESSOR DNA-BINDING DOMAIN, NMR, MINIMIZED STRUCTURE

1UXC の概要

• エントリーDOI: 10.2210/pdb1uxc/pdb
• 分子名称: FRUCTOSE REPRESSOR (1 entity in total)
• 機能のキーワード: dna-binding protein, fructose repressor, laci family, transcription regulation
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7396.48

構造登録者

Penin, F.,Geourjon, C.,Montserret, R.,Bockmann, A.,Lesage, A.,Yang, Y.,Bonod-Bidaud, C.,Cortay, J.C.,Negre, D.,Cozzone, A.J.,Deleage, G. (登録日: 1996-12-26, 公開日: 1997-04-21, 最終更新日: 2024-05-01)

主引用文献

Penin, F.,Geourjon, C.,Montserret, R.,Bockmann, A.,Lesage, A.,Yang, Y.S.,Bonod-Bidaud, C.,Cortay, J.C.,Negre, D.,Cozzone, A.J.,Deleage, G.
Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR.
J.Mol.Biol., 270:496-510, 1997

PubMed Abstract: FruR is an Escherichia coli transcriptional regulator that belongs to the LacI DNA-binding protein family. By using 1H and 15N NMR spectroscopy, we have determined the three-dimensional solution structure of the FruR N-terminal DNA-binding domain consisting of 57 amino acid residues. A total of 809 NMR-derived distances and 54 dihedral angle constraints have been used for molecular modelling with the X-PLOR program. The resulting set of calculated structures presents an average root-mean-square deviation of 0.37 A at the main-chain level for the first 47 residues. This highly defined N-terminal part of the structure reveals a similar topology for the three alpha-helices when compared to the 3D structures of LacI and PurR counterparts. The most striking difference lies in the connection between helix II and helix III, in which three additional residues are present in FruR. This connecting segment is well structured and contains a type III turn. Apart from hydrophobic interactions of non-polar residues with the core of the domain, this connecting segment is stabilised by several hydrogen bonds and by the aromatic ring stacking between Tyr19 of helix II and Tyr28 of the turn. The region containing the putative "hinge helix" (helix IV), that has been described in PurR-DNA complex to make specific base contacts in the minor groove of DNA, is unfolded. Examination of hydrogen bonds highlights the importance of homologous residues that seem to be conserved for their ability to fulfill helix N and C-capping roles in the LacI repressor family.

PubMed: 9237914
DOI: 10.1006/jmbi.1997.1123

実験手法

SOLUTION NMR