1B00

PHOB RECEIVER DOMAIN FROM ESCHERICHIA COLI

1B00 の概要

• エントリーDOI: 10.2210/pdb1b00/pdb
• 分子名称: PHOSPHATE REGULON TRANSCRIPTIONAL REGULATORY PROTEIN PHOB (2 entities in total)
• 機能のキーワード: transcription factor, phosphate regulation, activation of the pho regulon, alpha/beta doubly wound fold, gene regulation
• 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: 29031.51

構造登録者

Sola, M.,Gomis-Ruth, F.X.,Serrano, L.,Gonzalez, A.,Coll, M. (登録日: 1998-11-15, 公開日: 1999-11-19, 最終更新日: 2023-12-27)

主引用文献

Sola, M.,Gomis-Ruth, F.X.,Serrano, L.,Gonzalez, A.,Coll, M.
Three-dimensional crystal structure of the transcription factor PhoB receiver domain.
J.Mol.Biol., 285:675-687, 1999

PubMed Abstract: PhoB is the response regulator of the two-component signal transduction system activated under phosphate starvation conditions. This protein is a transcription factor that activates more than 30 genes of the pho regulon and consists of two domains: a DNA binding domain and a dimerization domain, the latter being homologous to the receiver domain described for two-component response regulators. Activation by phosphorylation induces dimerization of the protein and the consequent binding to the DNA direct repeat pho box, where it promotes the binding of RNA polymerase. In the absence of phosphorylation, the activating dimerization process can be mimicked by deletion of the DNA binding domain. The three-dimensional crystal structure of the receiver domain of PhoB from Escherichia coli has been solved by multiple anomalous diffraction using a gold derivative obtained by co-crystallization, and refined using data to 1.9 A resolution. The crystal structure reveals an alpha/beta doubly wound fold, similar to other known receivers, the most conspicuous difference being the displacement of helix alpha4 towards its N terminus. The active site includes the acidic triad Asp53 (the site of phosphorylation), Asp10 and Glu9. Lys105, from loop beta5alpha5, and Glu88, from helix alpha4, interact with Asp53 via an H-bond and a water bridge, respectively. In the asymmetric unit of the crystal there are two molecules linked by a complementary hydrophobic surface, which involves helix alpha1, loop beta5alpha5 and the N terminus of helix alpha5, and is connected to the active site through the fully conserved residue Lys105 from loop beta5alpha5. The possibility that this surface is the functional surface used for the activating dimerization is discussed.

PubMed: 9878437
DOI: 10.1006/jmbi.1998.2326

実験手法

X-RAY DIFFRACTION (1.88 Å)