PDBsum entry 4x23

Structural protein/DNA

PDB id: 4x23

Contents

Protein chains

95 a.a.

79 a.a.

102 a.a.

90 a.a.

22 a.a.

21 a.a.

DNA/RNA

Ligands

ASN-ARG-ILE-ARG-LEU

SER-ASN-ARG

PDB id:

4x23

Name:

Structural protein/DNA

Title:

Crystal structure of cenp-c in complex with the nucleosome core particle

Structure:

DNA (147-mer). Chain: i, s. Engineered: yes. Other_details: 147 bp widom 601 DNA fragment (+ strand). DNA (147-mer). Chain: j, t. Engineered: yes. Other_details: 147 bp widom 601 DNA fragment (- strand). Histone h3.

Source:

Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: his3. Gene: his4.

Resolution:

3.50Å R-factor: 0.238 R-free: 0.286

Authors:

J.S.Jiang

Key ref:

H.Kato et al. (2013). A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C. Science, 340, 1110-1113. PubMed id: 23723239 DOI: 10.1126/science.1235532

Date:

25-Nov-14 Release date: 10-Dec-14

Supersedes:

4inm

Protein chains

P02299  (H3_DROME) -  Histone H3 from Drosophila melanogaster

Seq: 136 a.a.

Struc: 95 a.a.*

Protein chains

P84040  (H4_DROME) -  Histone H4 from Drosophila melanogaster

Seq: 103 a.a.

Struc: 79 a.a.

Protein chains

P84051  (H2A_DROME) -  Histone H2A from Drosophila melanogaster

Seq: 124 a.a.

Struc: 102 a.a.

Protein chains

P02283  (H2B_DROME) -  Histone H2B from Drosophila melanogaster

Seq: 123 a.a.

Struc: 90 a.a.

Protein chain

Q66LH7  (Q66LH7_RAT) -  CENP-C from Rattus norvegicus

Seq: 916 a.a.

Struc: 22 a.a.

Protein chain

Q66LH7  (Q66LH7_RAT) -  CENP-C from Rattus norvegicus

Seq: 916 a.a.

Struc: 21 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chains

T-C-G-A-G-A-A-T-C-C-C-G-G-T-G-C-C-G-A-G-G-C-C-G-C-T-C-A-A-T-T-G-G-T-C-G-T-A-G- 146 bases

A-T-C-G-G-A-T-G-T-A-T-A-T-A-T-C-T-G-A-C-A-C-G-T-G-C-C-T-G-G-A-G-A-C-T-A-G-G-G- 146 bases

T-C-G-A-G-A-A-T-C-C-C-G-G-T-G-C-C-G-A-G-G-C-C-G-C-T-C-A-A-T-T-G-G-T-C-G-T-A-G- 146 bases

A-T-C-G-G-A-T-G-T-A-T-A-T-A-T-C-T-G-A-C-A-C-G-T-G-C-C-T-G-G-A-G-A-C-T-A-G-G-G- 146 bases

DOI no: 10.1126/science.1235532

Science 340:1110-1113 (2013)

PubMed id: 23723239

A conserved mechanism for centromeric nucleosome recognition by centromere protein CENP-C.

H.Kato, J.Jiang, B.R.Zhou, M.Rozendaal, H.Feng, R.Ghirlando, T.S.Xiao, A.F.Straight, Y.Bai.

ABSTRACT

Chromosome segregation during mitosis requires assembly of the kinetochore complex at the centromere. Kinetochore assembly depends on specific recognition of the histone variant CENP-A in the centromeric nucleosome by centromere protein C (CENP-C). We have defined the determinants of this recognition mechanism and discovered that CENP-C binds a hydrophobic region in the CENP-A tail and docks onto the acidic patch of histone H2A and H2B. We further found that the more broadly conserved CENP-C motif uses the same mechanism for CENP-A nucleosome recognition. Our findings reveal a conserved mechanism for protein recruitment to centromeres and a histone recognition mode whereby a disordered peptide binds the histone tail through hydrophobic interactions facilitated by nucleosome docking.