6AE8: Histone H2B.1,Histone H2A.Z

Name: PDB 6AE8: Structure insight into histone chaperone Chz1-mediated H2A.Z recognition and replacement
Published: 2019-04-17
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Structure insight into histone chaperone Chz1-mediated H2A.Z recognition and replacement. Determined by X-ray diffraction at 1.65 Å resolution. Released 17 Apr 2019.

Method: X-ray diffraction
Resolution: 1.65 Å
Organism: Saccharomyces cerevisiae S288c
Chains: 4
Atoms: 3,178
Mol. weight: 69.76 kDa
Ligands: BCN
Released: 17 Apr 2019

Explore 6AE8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6AE8 contains 26 α-helices and 12 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
α-helix	6-16	11
β-strand	21-22	2	1
β-strand	23	1	2
α-helix	24-51	28
β-strand	56-57	2	3
α-helix	59-69	11
α-helix	72-90	19
α-helix	98-101	4
α-helix	108-116	9
β-strand	124-125	2	3
α-helix	127-154	28
β-strand	159-160	2	1
α-helix	162-170	9
α-helix	173-181	9

Chain B: 10 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
α-helix	6-16	11
β-strand	21-22	2	4
β-strand	23	1	5
α-helix	24-51	28
β-strand	56-57	2	6
α-helix	59-69	11
α-helix	72-90	19
α-helix	98-101	4
α-helix	108-116	9
β-strand	124-125	2	6
α-helix	127-154	28
β-strand	159-160	2	4
α-helix	162-170	9
α-helix	173-180	8

Chains C and D: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	80-82	3
α-helix	86	1
β-strand	87	1	2
α-helix	88	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone H2B.1,Histone H2A.Z	A, B	protein	193	Saccharomyces cerevisiae S288c	P02293 (AlphaFold model), Q12692 (AlphaFold model)
Histone H2A.Z-specific chaperone CHZ1	C, D	protein	120	Saccharomyces cerevisiae S288c	P40019 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6AE8_1 Histone H2B.1,Histone H2A.Z (chains A, B)
MRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISA
REIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQAQSSSARAGLQFPVGRIKRYLKRHA
TGRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLI
RATIASGGVLPHI

Sequence of entity 2 (C, D), FASTA

>6AE8_2 Histone H2A.Z-specific chaperone CHZ1 (chains C, D)
MGSSHHHHHHYPYDVPDYASSGLVPRGSHMTVEDSESDMDDAKLDALMGNEGEEEEDDLA
EIDTSNIITSGRRTRGKVIDYKKTAEELDKKEPSTGSKDDVGYGEKEEDDEDEEDDDFKE

Ligands and cofactors

ID	Name	Formula	Copies
BCN	Bicine	C6 H13 N O4	2

Primary citation

Structural insights into histone chaperone Chz1-mediated H2A.Z recognition and histone replacement. Wang, Y., Liu, S., Sun, L. et al. PLoS Biol (2019) 17:e3000277-e3000277. DOI 10.1371/journal.pbio.3000277 · PubMed

Other PDB entries of the same protein (UniProt P02293 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4M6B 1.78 Å, Crystal structure of yeast Swr1-Z domain in complex with H2A.Z-H2B dimer
4WNN 1.8 Å, SPT16-H2A-H2B FACT HISTONE Complex
7DLX 2.4 Å, crystal structure of H2AM4>Z-H2B
5BT1 2.62 Å, histone chaperone Hif1 playing with histone H2A-H2B dimer
9C9G 2.91 Å, S.c INO80 in complex with S.c 0/80 nucleosome
9C9S 3.09 Å, S.c INO80 in complex with S.c 0/40 nucleosome, Class 1
7K78 3.1 Å, antibody and nucleosome complex
9C9T 3.16 Å, S.c INO80 in complex with S.c 0/40 nucleosome, Class 2
7SSA 3.2 Å, Cryo-EM structure of pioneer factor Cbf1 bound to the nucleosome
9OB1 3.2 Å, S.c INO80 in complex with Yeast 0/80 nucleosome, Apo State
4KUD 3.2 Å, Crystal structure of N-terminal acetylated Sir3 BAH domain D205N mutant in complex with…
7ON1 3.35 Å, Cenp-A nucleosome in complex with Cenp-C

Browse structure collections

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