1IGU

C-terminal Domain of the Transcriptional Repressor Protein KorB

1IGU の概要

• エントリーDOI: 10.2210/pdb1igu/pdb
• 関連するPDBエントリー: 1IGQ
• 分子名称: Transcriptional repressor protein KorB (2 entities in total)
• 機能のキーワード: sh3 domain, dimerization domain, transcription
• 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: 14220.04

構造登録者

Delbruck, H.,Heinemann, U. (登録日: 2001-04-18, 公開日: 2002-02-27, 最終更新日: 2023-08-16)

主引用文献

Delbruck, H.,Ziegelin, G.,Lanka, E.,Heinemann, U.
An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4.
J.Biol.Chem., 277:4191-4198, 2002

PubMed Abstract: KorB is a regulatory protein encoded by the conjugative plasmid RP4 and a member of the ParB family of bacterial partitioning proteins. The protein regulates the expression of plasmid genes whose products are involved in replication, transfer, and stable inheritance of RP4 by binding to palindromic 13-bp DNA sequences (5'-TTTAGC(G/C)GCTAAA-3') present 12 times in the 60-kb plasmid. Here we report the crystal structure of KorB-C, the C-terminal domain of KorB comprising residues 297-358. The structure of KorB-C was solved in two crystal forms. Quite unexpectedly, we find that KorB-C shows a fold closely resembling the Src homology 3 (SH3) domain, a fold well known from proteins involved in eukaryotic signal transduction. From the arrangement of molecules in the asymmetric unit, it is concluded that two molecules form a functionally relevant dimer. The detailed analysis of the dimer interface and a chemical cross-linking study suggest that the C-terminal domain is responsible for stabilizing the dimeric form of KorB in solution to facilitate binding to the palindromic operator sequence. The KorB-C crystal structure extends the range of protein-protein interactions known to be promoted by SH3 and SH3-like domains.

PubMed: 11711548
DOI: 10.1074/jbc.M110103200

実験手法

X-RAY DIFFRACTION (2.2 Å)