2P7C

Solution structure of the bacillus licheniformis BlaI monomeric form in complex with the blaP half-operator.

2P7C の概要

• エントリーDOI: 10.2210/pdb2p7c/pdb
• NMR情報: BMRB: 5873
• 分子名称: Strand 1 of Twelve base-pair DNA, Strand 2 of Twelve base-pair DNA, Penicillinase repressor (3 entities in total)
• 機能のキーワード: protein-dna complex, repressor, monomer, operator, antibiotics, transcription regulator
• 由来する生物種: Bacillus licheniformis; 詳細
• 細胞内の位置: Cytoplasm (Probable): P06555
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 16832.93

構造登録者

Boudet, J.,Duval, V.,Van Melckebeke, H.,Blackledge, M.,Amoroso, A.,Joris, B.,Simorre, J.-P. (登録日: 2007-03-20, 公開日: 2007-06-12, 最終更新日: 2024-05-22)

主引用文献

Boudet, J.,Duval, V.,Van Melckebeke, H.,Blackledge, M.,Amoroso, A.,Joris, B.,Simorre, J.P.
Conformational and thermodynamic changes of the repressor/DNA operator complex upon monomerization shed new light on regulation mechanisms of bacterial resistance against beta-lactam antibiotics.
Nucleic Acids Res., 35:4384-4395, 2007

PubMed Abstract: In absence of beta-lactam antibiotics, BlaI and MecI homodimeric repressors negatively control the expression of genes involved in beta-lactam resistance in Bacillus licheniformis and in Staphylococcus aureus. Subsequently to beta-lactam presence, BlaI/MecI is inactivated by a single-point proteolysis that separates its N-terminal DNA-binding domain to its C-terminal domain responsible for its dimerization. Concomitantly to this proteolysis, the truncated repressor acquires a low affinity for its DNA target that explains the expression of the structural gene for resistance. To understand the loss of the high DNA affinity of the truncated repressor, we have determined the different dissociation constants of the system and solved the solution structure of the B. licheniformis monomeric repressor complexed to the semi-operating sequence OP1 of blaP (1/2OP1blaP) by using a de novo docking approach based on inter-molecular nuclear Overhauser effects and chemical-shift differences measured on each macromolecular partner. Although the N-terminal domain of the repressor is not subject to internal structural rearrangements upon DNA binding, the molecules adopt a tertiary conformation different from the crystallographic operator-repressor dimer complex, leading to a 30 degrees rotation of the monomer with respect to a central axis extended across the DNA. These results open new insights for the repression and induction mechanisms of bacterial resistance to beta-lactams.

PubMed: 17576674
DOI: 10.1093/nar/gkm448

実験手法

SOLUTION NMR