2GLO

Solution structure of the Brinker DNA binding domain in complex with the omb enhancer

2GLO の概要

• エントリーDOI: 10.2210/pdb2glo/pdb
• NMR情報: BMRB: 7097
• 分子名称: 5'-D(*TP*GP*AP*GP*GP*CP*GP*TP*CP*AP*AP*C)-3', 5'-D(*GP*TP*TP*GP*AP*CP*GP*CP*CP*TP*CP*A)-3', brinker CG9653-PA (3 entities in total)
• 機能のキーワード: protein-dna complex, helix-turn-helix motif, transcription-dna complex, transcription/dna
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 14387.74

構造登録者

Cordier, F.,Hartmann, B.,Rogowski, M.,Affolter, M.,Grzesiek, S. (登録日: 2006-04-05, 公開日: 2006-08-29, 最終更新日: 2024-05-29)

主引用文献

Cordier, F.,Hartmann, B.,Rogowski, M.,Affolter, M.,Grzesiek, S.
DNA recognition by the brinker repressor - an extreme case of coupling between binding and folding
J.Mol.Biol., 361:659-672, 2006

PubMed Abstract: The Brinker (Brk) nuclear repressor is a major element of the Drosophila Decapentaplegic morphogen signaling pathway. Its N-terminal part has weak homology to the Antennapedia homeodomain and binds to GC-rich DNA sequences. We have investigated the conformation and dynamics of the N-terminal 101 amino acid residues of Brk in the absence and in the presence of cognate DNA by solution NMR spectroscopy. In the absence of DNA, Brk is unfolded and highly flexible throughout the entire backbone. Addition of cognate DNA induces the formation of a well-folded structure for residues R46 to R95. This structure consists of four helices forming a helix-turn-helix motif that differs from homeodomains, but has similarities to the Tc3 transposase, the Pax-6 Paired domain, and the human centromere-binding protein. The GC-rich DNA recognition can be explained by specific major groove hydrogen bonds from the N-terminal end of helix alpha3. The transition from a highly flexible, completely unfolded conformation in the absence of DNA to a well-formed structure in the complex presents a very extreme case of the "coupling of binding and folding" phenomenon.

PubMed: 16876822
DOI: 10.1016/j.jmb.2006.06.045

実験手法

SOLUTION NMR