PDBsum entry 4tzo

Peptide binding protein

PDB id: 4tzo

Contents

Protein chains

236 a.a.

14 a.a.

Waters ×283

PDB id:

4tzo

Name:

Peptide binding protein

Title:

Structure of c. Elegans htp-1 bound to him-3 closure motif

Structure:

Protein htp-1. Chain: a, c, e, g. Fragment: unp residues 1-253. Engineered: yes. Mutation: yes. C. Elegans him-3 closure motif. Chain: b, d, f, h. Fragment: unp residues 275-291. Synonym: protein him-3,isoform a.

Source:

Caenorhabditis elegans. Organism_taxid: 6239. Gene: htp-1, cele_f41h10.10, f41h10.10. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: him-3, cele_zk381.1, zk381.1.

Resolution:

2.40Å R-factor: 0.248 R-free: 0.282

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 chains

Q20305  (Q20305_CAEEL) -  HORMA domain-containing protein from Caenorhabditis elegans

Seq: 352 a.a.

Struc: 236 a.a.*

Protein chains

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

Seq: 291 a.a.

Struc: 14 a.a.*

* PDB and UniProt seqs differ at 2 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.