1HXD

CRYSTAL STRUCTURE OF E. COLI BIOTIN REPRESSOR WITH BOUND BIOTIN

1HXD の概要

• エントリーDOI: 10.2210/pdb1hxd/pdb
• 関連するPDBエントリー: 1BIA 1BIB
• 分子名称: BIRA BIFUNCTIONAL PROTEIN, BIOTIN (3 entities in total)
• 機能のキーワード: ligase, repressor, biotin, dna-binding
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71192.46

構造登録者

Kwon, K.,Streaker, E.D.,Ruparelia, S.,Beckett, D. (登録日: 2001-01-12, 公開日: 2001-05-30, 最終更新日: 2023-08-09)

主引用文献

Weaver, L.H.,Kwon, K.,Beckett, D.,Matthews, B.W.
Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
Proc.Natl.Acad.Sci.USA, 98:6045-6050, 2001

PubMed Abstract: The Escherichia coli biotin repressor binds to the biotin operator to repress transcription of the biotin biosynthetic operon. In this work, a structure determined by x-ray crystallography of a complex of the repressor bound to biotin, which also functions as an activator of DNA binding by the biotin repressor (BirA), is described. In contrast to the monomeric aporepressor, the complex is dimeric with an interface composed in part of an extended beta-sheet. Model building, coupled with biochemical data, suggests that this is the dimeric form of BirA that binds DNA. Segments of three surface loops that are disordered in the aporepressor structure are located in the interface region of the dimer and exhibit greater order than was observed in the aporepressor structure. The results suggest that the corepressor of BirA causes a disorder-to-order transition that is a prerequisite to repressor dimerization and DNA binding.

PubMed: 11353844
DOI: 10.1073/pnas.111128198

実験手法

X-RAY DIFFRACTION (2.4 Å)