3ISP

Crystal structure of ArgP from Mycobacterium tuberculosis

3ISP の概要

• エントリーDOI: 10.2210/pdb3isp/pdb
• 分子名称: HTH-type transcriptional regulator Rv1985c/MT2039 (2 entities in total)
• 機能のキーワード: rod shaped structure, dna binding domain, regulatory domain, dna-binding, transcription, transcription regulation
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65757.48

構造登録者

Zhou, X.,Lou, Z.,Sheng, F.,Bartlam, M.,Wang, H.,Rao, Z. (登録日: 2009-08-27, 公開日: 2010-02-16, 最終更新日: 2024-03-20)

主引用文献

Zhou, X.,Lou, Z.,Fu, S.,Yang, A.,Shen, H.,Li, Z.,Feng, Y.,Bartlam, M.,Wang, H.,Rao, Z.
Crystal Structure of ArgP from Mycobacterium tuberculosis Confirms Two Distinct Conformations of Full-length LysR Transcriptional Regulators and Reveals Its Function in DNA Binding and Transcriptional Regulation.
J.Mol.Biol., 2009

PubMed Abstract: Mycobacterium tuberculosis presents a challenging medical problem partly due to its persistent nonreplicative state. The inhibitor of chromosomal replication (iciA) protein encoded by M. tuberculosis has been suggested to inhibit chromosome replication initiation in vitro. However, iciA has also been identified as arginine permease (ArgP), a regulatory transcription factor for arginine outward transport. In order to understand the function of ArgP, we have determined its crystal structure by X-ray crystallography to a resolution of 2.7 A. ArgP is a member of the LysR-type transcriptional regulators (LTTRs) and forms a homodimer with each subunit containing two domains: a DNA binding domain (DBD) and a regulatory domain (RD). Two conformationally distinct subunits were identified: closed subunit and open subunit. This phenomenon was first observed in LTTR CbnR, but not in LTTR CrgA, and might be common in LTTRs. We identified two forms of dimers: DBD-type dimers and RD-type dimers. The former is confirmed in solution, and the latter is considered to form oligomers during function. We provide the first structural insights into the interaction of the extreme C-terminal residues with the DBD, which is confirmed by mutagenesis and analytical ultracentrifugation to be important for stability of the functional dimer. The structure serves as a model to suggest how three critical aspects, namely, DNA binding, homo-oligomerization, and interaction with RNAP, are mediated during regulation processing. A model is proposed for the LysR family of dimeric regulators.

PubMed: 20036253
DOI: 10.1016/j.jmb.2009.12.033

実験手法

X-RAY DIFFRACTION (2.7 Å)