PDBsum entry: 1g6z

Transferase

PDB id: 1g6z

Contents

Protein chain

70 a.a. *

* Residue conservation analysis

PDB id:

1g6z

Name:

Transferase

Title:

Solution structure of the clr4 chromo domain

Structure:

Clr4 protein. Chain: a. Fragment: chromo domain, residues 2-69. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: clr4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

25 models

Authors:

D.A.Horita,A.V.Ivanova,A.S.Altieri,A.J.Klar,R.A.Byrd

Key ref:

D.A.Horita et al. (2001). Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4. J Mol Biol, 307, 861-870. PubMed id: 11273706 DOI: 10.1006/jmbi.2001.4515

Date:

08-Nov-00 Release date: 04-Apr-01

Protein chain

O60016  (CLR4_SCHPO) -  Histone-lysine N-methyltransferase, H3 lysine-9 specific

Seq: 490 a.a.

Struc: 70 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.1.1.43 - Histone-lysine N-methyltransferase.
• Reaction: S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N₆-methyl-L-lysine-[histone]

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: chromatin assembly or disassembly (2 terms)
• Biochemical function: chromatin binding (2 terms)

Added reference

DOI no: 10.1006/jmbi.2001.4515

J Mol Biol 307:861-870 (2001)

PubMed id: 11273706

Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4.

D.A.Horita, A.V.Ivanova, A.S.Altieri, A.J.Klar, R.A.Byrd.

ABSTRACT

The encapsulation of otherwise transcribable loci within transcriptionally inactive heterochromatin is rapidly gaining recognition as an important mechanism of epigenetic gene regulation. In the fission yeast Schizosaccharomyces pombe, heterochromatinization of the mat2/mat3 loci silences the mating-type information encoded within these loci. Here, we present the solution structure of the chromo domain from the cryptic loci regulator protein Clr4. Clr4 is known to regulate silencing and switching at the mating-type loci and to affect chromatin structure at centromeres. Clr4 and its human and Drosophila homologs have been identified as histone H3-specific methyltransferases, further implicating this family of proteins in chromatin remodeling. Our structure highlights a conserved surface that may be involved in chromo domain-ligand interactions. We have also analyzed two chromo domain mutants (W31G and W41G) that previously were shown to affect silencing and switching in full-length Clr4. Both mutants are significantly destabilized relative to wild-type.

Selected figure(s)

Figure 2.
Figure 2. Structure of the Clr4 chromo domain. (a) Overlay of 25 low-energy structures. (b) Ribbon diagram (in stereo) of a single structure. The N and C termini are disordered, as is the b[2]b[3] loop.

Figure 5.
Figure 5. (a) CPK and (b) ball-and-stick representations of the conserved non-core residues of chromo domains mapped onto Clr4. Core residues and non-conserved surface residues are colored light green. The conserved, surface-exposed residues form a contiguous patch which extends from the hydrophobic groove around the edge of the b-sheet. Structures in (a) and (b) are shown in identical orientations.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 307, 861-870) copyright 2001.

Figures were selected by the author.