3E5U

OCPA complexed CprK (C200S)

3E5U の概要

• エントリーDOI: 10.2210/pdb3e5u/pdb
• 関連するPDBエントリー: 3E5Q 3E5X 3E6B 3E6C 3E6D
• 分子名称: Cyclic nucleotide-binding protein, (3-CHLORO-4-HYDROXYPHENYL)ACETIC ACID, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: cprk, halorespiration, transcriptional regulator, transcription regulation
• 由来する生物種: Desulfitobacterium hafniense
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114759.33

構造登録者

Levy, C. (登録日: 2008-08-14, 公開日: 2008-09-30, 最終更新日: 2024-02-21)

主引用文献

Levy, C.,Pike, K.,Heyes, D.J.,Joyce, M.G.,Gabor, K.,Smidt, H.,van der Oost, J.,Leys, D.
Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator
Mol.Microbiol., 70:151-167, 2008

PubMed Abstract: Certain bacteria are able to conserve energy via the reductive dehalogenation of halo-organic compounds in a respiration-type metabolism. The transcriptional regulator CprK from Desulfitobacterium spp. induces expression of halorespiratory genes upon binding of o-chlorophenol ligands and is reversibly inactivated by oxygen through disulphide bond formation. We report crystal structures of D. hafniense CprK in the ligand-free (both oxidation states), ligand-bound (reduced) and DNA-bound states, making it the first member of the widespread CRP-FNR superfamily for which a complete structural description of both redox-dependent and allosteric molecular rearrangements is available. In conjunction with kinetic and thermodynamic ligand binding studies, we provide a model for the allosteric mechanisms underpinning transcriptional control. Amino acids that play a key role in this mechanism are not conserved in functionally distinct CRP-FNR members. This suggests that, despite significant structural homology, distinct allosteric mechanisms are used, enabling this protein family to control a very wide range of processes.

PubMed: 18717788
DOI: 10.1111/j.1365-2958.2008.06399.x

実験手法

X-RAY DIFFRACTION (1.83 Å)