6vo5

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Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4

Structural highlights

6vo5 is a 4 chain structure. This structure supersedes the now removed PDB entry 6uhd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
NonStd Res:
Activity:Histone acetyltransferase, with EC number 2.3.1.48
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HAT1_HUMAN] Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage.[1] [2] [3]

References

  1. Verreault A, Kaufman PD, Kobayashi R, Stillman B. Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr Biol. 1998 Jan 15;8(2):96-108. PMID:9427644
  2. Makowski AM, Dutnall RN, Annunziato AT. Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase. J Biol Chem. 2001 Nov 23;276(47):43499-502. Epub 2001 Oct 3. PMID:11585814 doi:http://dx.doi.org/10.1074/jbc.C100549200
  3. Campos EI, Fillingham J, Li G, Zheng H, Voigt P, Kuo WH, Seepany H, Gao Z, Day LA, Greenblatt JF, Reinberg D. The program for processing newly synthesized histones H3.1 and H4. Nat Struct Mol Biol. 2010 Nov;17(11):1343-51. doi: 10.1038/nsmb.1911. Epub 2010, Oct 17. PMID:20953179 doi:http://dx.doi.org/10.1038/nsmb.1911

6vo5, resolution 1.60Å

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