PDBsum entry 2mh2

DNA binding protein

PDB id: 2mh2

Contents

Protein chain

64 a.a.

PDB id:

2mh2

Name:

DNA binding protein

Title:

Structural insights into the DNA recognition and protein interaction domains reveal fundamental homologous DNA pairing properties of hop2

Structure:

Homologous-pairing protein 2 homolog. Chain: a. Fragment: n-terminal domain (unp residues 1-84). Synonym: hop2, psmc3-interacting protein, proteasome 26s atpase subunit 3-interacting protein, tat-binding protein 1-interacting protein, tbp-1-interacting protein. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: hop2, psmc3ip, tbpip. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

H.Moktan,M.F.Guiraldelli,C.A.Eyter,W.Zhao,R.D.Camerini-Otero,P.Sung, D.H.Zhou,R.J.Pezza

Key ref:

H.Moktan et al. (2014). Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein. J Biol Chem, 289, 14682-14691. PubMed id: 24711446 DOI: 10.1074/jbc.M114.548180

Date:

13-Nov-13 Release date: 16-Apr-14

Protein chain

O35047  (HOP2_MOUSE) -  Homologous-pairing protein 2 homolog from Mus musculus

Seq: 217 a.a.

Struc: 64 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M114.548180

J Biol Chem 289:14682-14691 (2014)

PubMed id: 24711446

Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein.

H.Moktan, M.F.Guiraldelli, C.A.Eyster, W.Zhao, C.Y.Lee, T.Mather, R.D.Camerini-Otero, P.Sung, D.H.Zhou, R.J.Pezza.

ABSTRACT

The HOP2 protein is required for efficient double-strand break repair which ensures the proper synapsis of homologous chromosomes and normal meiotic progression. We previously showed that in vitro HOP2 shows two distinctive activities: when it is incorporated into a HOP2-MND1 heterodimer, it stimulates DMC1 and RAD51 recombination activities, and the purified HOP2 alone is proficient in promoting strand invasion. The structural and biochemical basis of HOP2 action in recombination are poorly understood; therefore, they are the focus of this work. Herein, we present the solution structure of the amino-terminal portion of mouse HOP2, which contains a typical winged helix DNA-binding domain. Together with NMR spectral changes in the presence of double-stranded DNA, protein docking on DNA, and mutation analysis to identify the amino acids involved in DNA coordination, our results on the three-dimensional structure of HOP2 provide key information on the fundamental structural and biochemical requirements directing the interaction of HOP2 with DNA. These results, in combination with mutational experiments showing the role of a coiled-coil structural feature involved in HOP2 self-association, allow us to explain important aspects of the function of HOP2 in recombination.