PDBsum entry 3fss

Chaperone

PDB id

3fss

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Contents

			Protein chain

					222 a.a. *

			Ligands

					GOL ×3


					MLA

			Waters ×378

* Residue conservation analysis

PDB id:

3fss

Links

Name:

Chaperone

Title:

Structure of the tandem ph domains of rtt106

Structure:

Histone chaperone rtt106. Chain: a. Fragment: unp residues 68-301, histone binding segment. Synonym: regulator of ty1 transposition protein 106. Engineered: yes. Mutation: yes

Source:

Saccharomyces cerevisiae. Baker's yeast, yeast. Organism_taxid: 4932. Gene: n1346, rtt106, ynl206c. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.43Å

R-factor:

0.182

R-free:

0.210

Authors:

D.Su,J.R.Thompson,G.Mer

Key ref:

D.Su et al. (2012). Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. Nature, 483, 104-107. PubMed id: 22307274

Date:

11-Jan-09

Release date:

22-Dec-09

PROCHECK

	Headers

	References

Protein chain

P40161 (RT106_YEAST) - Histone chaperone RTT106 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:					455 a.a. 222 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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

	Nature 483:104-107 (2012)
PubMed id: 22307274

Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.
D.Su, Q.Hu, Q.Li, J.R.Thompson, G.Cui, A.Fazly, B.A.Davies, M.V.Botuyan, Z.Zhang, G.Mer.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

23288364

R.J.Burgess, and Z.Zhang (2013).
Histone chaperones in nucleosome assembly and human disease.

Nat Struct Mol Biol, 20, 14-22.

23211769

C.A.Musselman, M.E.Lalonde, J.Côté, and T.G.Kutateladze (2012).
Perceiving the epigenetic landscape through histone readers.

Nat Struct Mol Biol, 19, 1218-1227.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.