1WRP

FLEXIBILITY OF THE DNA-BINDING DOMAINS OF TRP REPRESSOR

1WRP の概要

• エントリーDOI: 10.2210/pdb1wrp/pdb
• 関連するPDBエントリー: 1WRP 3WRP
• 分子名称: TRP REPRESSOR, TRYPTOPHAN (3 entities in total)
• 機能のキーワード: dna binding regulatory protein
• 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: 12443.16

構造登録者

Schewitz, R.W.,Otwinowski, Z.,Lawson, C.L.,Joachimiak, A.,Sigler, P.B. (登録日: 1987-12-01, 公開日: 1988-04-16, 最終更新日: 2024-02-14)

主引用文献

Lawson, C.L.,Zhang, R.G.,Schevitz, R.W.,Otwinowski, Z.,Joachimiak, A.,Sigler, P.B.
Flexibility of the DNA-binding domains of trp repressor.
Proteins, 3:18-31, 1988

PubMed Abstract: An orthorhombic crystal form of trp repressor (aporepressor plus L-tryptophan ligand) was solved by molecular replacement, refined to 1.65 A resolution, and compared to the structure of the repressor in trigonal crystals. Even though these two crystal forms of repressor were grown under identical conditions, the refined structures have distinctly different conformations of the DNA-binding domains. Unlike the repressor/aporepressor structural transition, the conformational shift is not caused by the binding or loss of the L-tryptophan ligand. We conclude that while L-tryptophan binding is essential for forming a specific complex with trp operator DNA, the corepressor ligand does not lock the repressor into a single conformation that is complementary to the operator. This flexibility may be required by the various binding modes proposed for trp repressor in its search for and adherence to its three different operator sites.

PubMed: 3375234
DOI: 10.1002/prot.340030103

実験手法

X-RAY DIFFRACTION (2.2 Å)