5ZR4

Manganese-dependent transcriptional repressor

Summary for 5ZR4

• Entry DOI: 10.2210/pdb5zr4/pdb
• Descriptor: Metal-dependent transcriptional regulator (2 entities in total)
• Functional Keywords: transcriptional repressor, transcription
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 49964.38

Authors

Cong, X.Y.,Gu, L.C.,Wang, J.B. (deposition date: 2018-04-23, release date: 2019-01-23, Last modification date: 2024-03-27)

Primary citation

Cong, X.Y.,Yuan, Z.L.,Wang, Z.,Wei, B.,Xu, S.J.,Wang, J.B.
Crystal structures of manganese-dependent transcriptional repressor MntR (Rv2788) from Mycobacterium tuberculosis in apo and manganese bound forms.
Biochem. Biophys. Res. Commun., 501:423-427, 2018

PubMed Abstract: The pathogenic Mycobacterium tuberculosis encodes two members of the DtxR family metalloregulators, IdeR and MntR. IdeR represses gene expression in response to ferrous iron, while MntR (Rv2788) functions as a manganese-dependent transcriptional repressor, which represses the expression of manganese transporter genes to maintain manganese homeostasis. Although the structural study towards IdeR is in-depth, there is no MntR structure available. Herein, we report both apo and manganese bound forms of MntR structures from M. tuberculosis. MntR has evolved into two metal ion binding sites like other DtxR proteins and for the first time, we captured the two sites fully occupied by its natural ions with one Mn ion at the first site and two Mn ions at the second binding site (binuclear manganese cluster). The conformation change of MntR resulting from manganese binding could prime the MntR for DNA binding, which is a conserved activation mechanism among DtxR family.

PubMed: 29730293
DOI: 10.1016/j.bbrc.2018.05.005

Experimental method

X-RAY DIFFRACTION (3.1 Å)