PDBsum entry 4tzj

Peptide binding protein

PDB id: 4tzj

Contents

Protein chain

242 a.a.

PDB id:

4tzj

Name:

Peptide binding protein

Title:

Structure of c. Elegans him-3 bound to htp-3 closure motif-4

Structure:

C. Elegans him-3 and htp-3. Chain: a. Fragment: unp g5ebg0 residues 1-276,unp o01820 residues 649-663. Engineered: yes. Other_details: chimera

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: him-3, cele_zk381.1, zk381.1, htp-3, cele_f57c9.5, f57c9.5. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.85Å R-factor: 0.180 R-free: 0.230

Authors:

S.C.Rosenberg,K.D.Corbett

Key ref:

Y.Kim et al. (2014). The chromosome axis controls meiotic events through a hierarchical assembly of HORMA domain proteins. Dev Cell, 31, 487-502. PubMed id: 25446517 DOI: 10.1016/j.devcel.2014.09.013

Date:

10-Jul-14 Release date: 19-Nov-14

Protein chain

G5EBG0  (G5EBG0_CAEEL) -  HORMA domain-containing protein from Caenorhabditis elegans

Seq: 291 a.a.

Struc: 242 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

DOI no: 10.1016/j.devcel.2014.09.013

Dev Cell 31:487-502 (2014)

PubMed id: 25446517

The chromosome axis controls meiotic events through a hierarchical assembly of HORMA domain proteins.

Y.Kim, S.C.Rosenberg, C.L.Kugel, N.Kostow, O.Rog, V.Davydov, T.Y.Su, A.F.Dernburg, K.D.Corbett.

ABSTRACT

Proteins of the HORMA domain family play central, but poorly understood, roles in chromosome organization and dynamics during meiosis. In Caenorhabditis elegans, four such proteins (HIM-3, HTP-1, HTP-2, and HTP-3) have distinct but overlapping functions. Through combined biochemical, structural, and in vivo analysis, we find that these proteins form hierarchical complexes through binding of their HORMA domains to cognate peptides within their partners' C-terminal tails, analogous to the "safety belt" binding mechanism of Mad2. These interactions are critical for recruitment of HIM-3, HTP-1, and HTP-2 to chromosome axes. HTP-3, in addition to recruiting the other HORMA domain proteins to the axis, plays an independent role in sister chromatid cohesion and double-strand break formation. Finally, we find that mammalian HORMAD1 binds a motif found both at its own C terminus and at that of HORMAD2, indicating that this mode of intermolecular association is a conserved feature of meiotic chromosome structure in eukaryotes.