4B09

Structure of unphosphorylated BaeR dimer

4B09 の概要

• エントリーDOI: 10.2210/pdb4b09/pdb
• 分子名称: TRANSCRIPTIONAL REGULATORY PROTEIN BAER, HEXATANTALUM DODECABROMIDE (2 entities in total)
• 機能のキーワード: transcription, response regulator, dna binding
• 由来する生物種: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655
• 細胞内の位置: Cytoplasm (Potential): P69229
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 353572.89

構造登録者

Choudhury, H.,Beis, K. (登録日: 2012-06-29, 公開日: 2013-07-10, 最終更新日: 2024-11-13)

主引用文献

Choudhury, H.G.,Beis, K.
The Dimeric Form of the Unphosphorylated Response Regulator Baer.
Protein Sci., 22:1287-, 2013

PubMed Abstract: Bacterial response regulators (RRs) can regulate the expression of genes that confer antibiotic resistance; they contain a receiver and an effector domain and their ability to bind DNA is based on the dimerization state. This is triggered by phosphorylation of the receiver domain by a kinase. However, even in the absence of phosphorylation RRs can exist in equilibrium between monomers and dimers with phosphorylation shifting the equilibrium toward the dimer form. We have determined the crystal structure of the unphosphorylated dimeric BaeR from Escherichia coli. The dimer interface is formed by a domain swap at the receiver domain. In comparison with the unphosphorylated dimeric PhoP from Mycobacterium tuberculosis, BaeR displays an asymmetry of the effector domains.

PubMed: 23868292
DOI: 10.1002/PRO.2311

実験手法

X-RAY DIFFRACTION (3.3 Å)