PDBsum entry 4xdn

Cell cycle

PDB id: 4xdn

Contents

Protein chains

604 a.a.

122 a.a.

Ligands

SO4 ×5

Waters ×301

PDB id:

4xdn

Name:

Cell cycle

Title:

Crystal structure of scc4 in complex with scc2n

Structure:

Mau2 chromatid cohesion factor homolog. Chain: a. Synonym: sister chromatid cohesion protein 4. Engineered: yes. Sister chromatid cohesion protein 2. Chain: b. Fragment: n-terminal region (unp residues 1-181). Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: scc4. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: scc2. Expression_system_taxid: 562

Resolution:

2.08Å R-factor: 0.186 R-free: 0.210

Authors:

S.M.Hinshaw,S.C.Harrison

Key ref:

S.M.Hinshaw et al. (2015). Structural evidence for Scc4-dependent localization of cohesin loading. Elife, 4, e06057. PubMed id: 26038942 DOI: 10.7554/eLife.06057

Date:

19-Dec-14 Release date: 17-Jun-15

Protein chain

P40090  (SCC4_YEAST) -  MAU2 chromatid cohesion factor homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 624 a.a.

Struc: 604 a.a.

Protein chain

Q04002  (SCC2_YEAST) -  Sister chromatid cohesion protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1493 a.a.

Struc: 122 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.7554/eLife.06057

Elife 4:e06057 (2015)

PubMed id: 26038942

Structural evidence for Scc4-dependent localization of cohesin loading.

S.M.Hinshaw, V.Makrantoni, A.Kerr, A.L.Marston, S.C.Harrison.

ABSTRACT

The cohesin ring holds newly replicated sister chromatids together until their separation at anaphase. Initiation of sister chromatid cohesion depends on a separate complex, Scc2(NIPBL)/Scc4(Mau2) (Scc2/4), which loads cohesin onto DNA and determines its localization across the genome. Proper cohesin loading is essential for cell division, and partial defects cause chromosome missegregation and aberrant transcriptional regulation, leading to severe developmental defects in multicellular organisms. We present here a crystal structure showing the interaction between Scc2 and Scc4. Scc4 is a TPR array that envelops an extended Scc2 peptide. Using budding yeast, we demonstrate that a conserved patch on the surface of Scc4 is required to recruit Scc2/4 to centromeres and to build pericentromeric cohesion. These findings reveal the role of Scc4 in determining the localization of cohesin loading and establish a molecular basis for Scc2/4 recruitment to centromeres.