PDBsum entry 3w98

Structural protein/DNA

PDB id: 3w98

Contents

Protein chains

97 a.a.

76 a.a.

106 a.a.

95 a.a.

84 a.a.

DNA/RNA

Metals

_MN

PDB id:

3w98

Name:

Structural protein/DNA

Title:

Crystal structure of human nucleosome core particle lacking h3.1 n- terminal region

Structure:

Histone h3.1. Chain: a, e. Fragment: unp residues 29-136. Synonym: histone h3/a, histone h3/b, histone h3/c, histone h3/d, histone h3/f, histone h3/h, histone h3/i, histone h3/j, histone h3/k, histone h3/l. Engineered: yes. Histone h4. Chain: b, f.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: hist1h3a, h3fa, hist1h3b, h3fl, hist1h3c, h3fc, hist1h3d, h3fb, hist1h3e, h3fd, hist1h3f, h3fi, hist1h3g, h3fh, hist1h3h, h3fk, hist1h3i, h3ff, hist1h3j, h3fj. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hist1h4a, h4/a, h4fa, hist1h4b, h4/i, h4fi, hist1h4c, h4/g,

Resolution:

3.42Å R-factor: 0.260 R-free: 0.303

Authors:

W.Iwasaki,Y.Miya,N.Horikoshi,A.Osakabe,H.Tachiwana,T.Shibata, W.Kagawa,H.Kurumizaka

Key ref:

W.Iwasaki et al. (2013). Contribution of histone N-terminal tails to the structure and stability of nucleosomes. Febs Open Bio, 3, 363-369. PubMed id: 24251097 DOI: 10.1016/j.fob.2013.08.007

Date:

01-Apr-13 Release date: 28-Aug-13

Protein chains

P68431  (H31_HUMAN) -  Histone H3.1 from Homo sapiens

Seq: 136 a.a.

Struc: 97 a.a.

Protein chain

P62805  (H4_HUMAN) -  Histone H4 from Homo sapiens

Seq: 103 a.a.

Struc: 76 a.a.

Protein chains

P04908  (H2A1B_HUMAN) -  Histone H2A type 1-B/E from Homo sapiens

Seq: 130 a.a.

Struc: 106 a.a.

Protein chains

P06899  (H2B1J_HUMAN) -  Histone H2B type 1-J from Homo sapiens

Seq: 126 a.a.

Struc: 95 a.a.

Protein chain

P62805  (H4_HUMAN) -  Histone H4 from Homo sapiens

Seq: 103 a.a.

Struc: 84 a.a.

DNA/RNA chains

A-T-C-A-A-T-A-T-C-C-A-C-C-T-G-C-A-G-A-T-T-C-T-A-C-C-A-A-A-A-G-T-G-T-A-T-T-T-G- 145 bases

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

DOI no: 10.1016/j.fob.2013.08.007

Febs Open Bio 3:363-369 (2013)

PubMed id: 24251097

Contribution of histone N-terminal tails to the structure and stability of nucleosomes.

W.Iwasaki, Y.Miya, N.Horikoshi, A.Osakabe, H.Taguchi, H.Tachiwana, T.Shibata, W.Kagawa, H.Kurumizaka.

ABSTRACT

Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure.