PDBsum entry 6tob

DNA binding protein

PDB id: 6tob

Contents

Protein chain

109 a.a.

PDB id:

6tob

Name:

DNA binding protein

Title:

Structural and DNA binding properties of mycobacterial integration host factor mihf

Structure:

Integration host factor mihf. Chain: a. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: mihf, ers007672_05099, ers007703_04035. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

20 models

Authors:

T.Herrmann

Key ref:

N.T.Odermatt et al. (2020). Structural and DNA binding properties of mycobacterial integration host factor mIHF. J Struct Biol, 209, 107434. PubMed id: 31846718 DOI: 10.1016/j.jsb.2019.107434

Date:

11-Dec-19 Release date: 25-Dec-19

Protein chain

P71658  (IHF_MYCTU) -  Integration host factor from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 105 a.a.

Struc: 109 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jsb.2019.107434

J Struct Biol 209:107434 (2020)

PubMed id: 31846718

Structural and DNA binding properties of mycobacterial integration host factor mIHF.

N.T.Odermatt, M.Lelli, T.Herrmann, L.A.Abriata, A.Japaridze, H.Voilquin, R.Singh, J.Piton, L.Emsley, G.Dietler, S.T.Cole.

ABSTRACT

In bacteria, nucleoid associated proteins (NAPs) take part in active chromosome organization by supercoil management, three-dimensional DNA looping and direct transcriptional control. Mycobacterial integration host factor (mIHF, rv1388) is a NAP restricted to Actinobacteria and essential for survival of the human pathogen Mycobacterium tuberculosis. We show in vitro that DNA binding by mIHF strongly stabilizes the protein and increases its melting temperature. The structure obtained by Nuclear Magnetic Resonance (NMR) spectroscopy characterizes mIHF as a globular protein with a protruding alpha helix and a disordered N-terminus, similar to Streptomyces coelicolor IHF (sIHF). NMR revealed no residues of high flexibility, suggesting that mIHF is a rigid protein overall that does not undergo structural rearrangements. We show that mIHF only binds to double stranded DNA in solution, through two DNA binding sites (DBSs) similar to those identified in the X-ray structure of sIHF. According to Atomic Force Microscopy, mIHF is able to introduce left-handed loops of ca. 100 nm size (~300 bp) in supercoiled cosmids, thereby unwinding and relaxing the DNA.