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Acetyltransferase PDB id
1bob
Jmol
Contents
Protein chain
306 a.a. *
Ligands
ACO
Metals
_CA
Waters ×112
* Residue conservation analysis
PDB id:
1bob
Name: Acetyltransferase
Title: Histone acetyltransferase hat1 from saccharomyces cerevisiae in complex with acetyl coenzyme a
Structure: Histone acetyltransferase. Chain: a. Synonym: hat1. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Cell_line: b834. Cellular_location: nucleus. Gene: hat1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Monomer (from PDB file)
Resolution:
2.30Å     R-factor:   0.204     R-free:   0.269
Authors: R.N.Dutnall,S.T.Tafrov,R.Sternglanz,V.Ramakrishnan
Key ref:
R.N.Dutnall et al. (1998). Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell, 94, 427-438. PubMed id: 9727486 DOI: 10.1016/S0092-8674(00)81584-6
Date:
02-Jul-98     Release date:   20-Apr-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q12341  (HAT1_YEAST) -  Histone acetyltransferase type B catalytic subunit
Seq:
Struc: 		374 a.a.
306 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.48  - Histone acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Acetyl-CoA + [histone] = CoA + acetyl-[histone]
Acetyl-CoA
Bound ligand (Het Group name = ACO)
corresponds exactly 		+ [histone]
 = CoA
 + acetyl-[histone]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     histone acetyltransferase complex   1 term 
  Biological process     metabolic process   4 terms 
  Biochemical function     protein binding     3 terms  

 

 
    Added reference    
 
 
DOI no: 10.1016/S0092-8674(00)81584-6 Cell 94:427-438 (1998)
PubMed id: 9727486  
 
 
Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
R.N.Dutnall, S.T.Tafrov, R.Sternglanz, V.Ramakrishnan.
 
  ABSTRACT  
 
We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate. A model for histone H4 binding by Hat1 is discussed in terms of possible sources of specific lysine recognition by the enzyme. The structure of Hat1 provides a model for the structures of the catalytic domains of a protein superfamily that includes other histone acetyltransferases such as Gcn5 and CBP.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Overview of the Structure of the Hat1–AcCoA ComplexSchematic representation of the structure showing location of sheets and helices. The AcCoA molecule is indicated in a ball-and-stick representation. Two views of the structure are shown, related by an approximately 90° turn around the vertical axis. Figure produced using MOLSCRIPT ([21]) and Raster3D ( [26]). 		Figure 4.
Figure 4. Model of Histone H4 Tail Binding Suggests How a Complementary Fit May Explain Substrate Recognition by Hat1An electrostatic surface potential of the Hat1–AcCoA complex is shown along with a stick representation of the AcCoA and H4 peptide (residues 6–19). The surface is partially transparent to show the location of the acetyl group and the side chain of Lys-12 positioned for modification. The surface features of Hat1 that may play a role in substrate recognition are indicated.
 
  The above figures are reprinted by permission from Cell Press: Cell (1998, 94, 427-438) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21243716 B.N.Albaugh, K.M.Arnold, and J.M.Denu (2011).
KAT(ching) metabolism by the tail: insight into the links between lysine acetyltransferases and metabolism.
  Chembiochem, 12, 290-298.  
19889644 K.Oda, Y.Matoba, M.Noda, T.Kumagai, and M.Sugiyama (2010).
Catalytic mechanism of bleomycin N-acetyltransferase proposed on the basis of its crystal structure.
  J Biol Chem, 285, 1446-1456.
PDB codes: 2zw4 2zw5 2zw6 2zw7
19692582 I.Onn, V.Guacci, and D.E.Koshland (2009).
The zinc finger of Eco1 enhances its acetyltransferase activity during sister chromatid cohesion.
  Nucleic Acids Res, 37, 6126-6134.  
19779690 K.B.Falbo, and X.Shen (2009).
Histone modifications during DNA replication.
  Mol Cells, 28, 149-154.  
18794801 A.Ametzazurra, E.Larrea, M.P.Civeira, J.Prieto, and R.Aldabe (2008).
Implication of human N-alpha-acetyltransferase 5 in cellular proliferation and carcinogenesis.
  Oncogene, 27, 7296-7306.  
18373695 A.Poveda, and R.Sendra (2008).
Site specificity of yeast histone acetyltransferase B complex in vivo.
  FEBS J, 275, 2122-2136.  
18753131 E.L.Mersfelder, and M.R.Parthun (2008).
Involvement of Hat1p (Kat1p) catalytic activity and subcellular localization in telomeric silencing.
  J Biol Chem, 283, 29060-29068.  
18709443 J.R.Cort, T.A.Ramelot, D.Murray, T.B.Acton, L.C.Ma, R.Xiao, G.T.Montelione, and M.A.Kennedy (2008).
Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.
  J Struct Funct Genomics, 9, 7.
PDB codes: 1r57 2h5m
18373682 T.Kotani, and H.Takagi (2008).
Identification of amino acid residues essential for the yeast N-acetyltransferase Mpr1 activity by site-directed mutagenesis.
  FEMS Yeast Res, 8, 607-614.  
18541056 Y.L.Chang, H.K.Tsai, C.Y.Kao, Y.C.Chen, Y.J.Hu, and J.M.Yang (2008).
Evolutionary conservation of DNA-contact residues in DNA-binding domains.
  BMC Bioinformatics, 9, S3.  
17410582 A.Schuetz, G.Bernstein, A.Dong, T.Antoshenko, H.Wu, P.Loppnau, A.Bochkarev, and A.N.Plotnikov (2007).
Crystal structure of a binary complex between human GCN5 histone acetyltransferase domain and acetyl coenzyme A.
  Proteins, 68, 403-407.
PDB code: 1z4r
17052979 L.J.Benson, J.A.Phillips, Y.Gu, M.R.Parthun, C.S.Hoffman, and A.T.Annunziato (2007).
Properties of the type B histone acetyltransferase Hat1: H4 tail interaction, site preference, and involvement in DNA repair.
  J Biol Chem, 282, 836-842.  
17694075 M.R.Parthun (2007).
Hat1: the emerging cellular roles of a type B histone acetyltransferase.
  Oncogene, 26, 5319-5328.  
17039546 N.Nagano, T.Noguchi, and Y.Akiyama (2007).
Systematic comparison of catalytic mechanisms of hydrolysis and transfer reactions classified in the EzCatDB database.
  Proteins, 66, 147-159.  
17272722 R.Driscoll, A.Hudson, and S.P.Jackson (2007).
Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56.
  Science, 315, 649-652.  
17984971 S.Lall (2007).
Primers on chromatin.
  Nat Struct Mol Biol, 14, 1110-1115.  
16356930 C.A.Toleman, A.J.Paterson, and J.E.Kudlow (2006).
The histone acetyltransferase NCOAT contains a zinc finger-like motif involved in substrate recognition.
  J Biol Chem, 281, 3918-3925.  
17128971 R.C.Tyler, E.Bitto, C.E.Berndsen, C.A.Bingman, S.Singh, M.S.Lee, G.E.Wesenberg, J.M.Denu, G.N.Phillips, and J.L.Markley (2006).
Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family.
  Biochemistry, 45, 14325-14336.
PDB codes: 1xmt 2evn 2gdb 2il4
15980378 A.Pourreza, M.Witherspoon, J.Fox, J.Newmark, D.Bui, and M.E.Tolmasky (2005).
Mutagenesis analysis of a conserved region involved in acetyl coenzyme A binding in the aminoglycoside 6'-N-acetyltransferase type Ib encoded by plasmid pJHCMW1.
  Antimicrob Agents Chemother, 49, 2979-2982.  
16131761 D.L.Burk, B.Xiong, C.Breitbach, and A.M.Berghuis (2005).
Structures of aminoglycoside acetyltransferase AAC(6')-Ii in a novel crystal form: structural and normal-mode analyses.
  Acta Crystallogr D Biol Crystallogr, 61, 1273-1279.
PDB code: 2a4n
18248177 J.H.Tan, S.I.Quek, and W.K.Chan (2005).
Cloning, Genomic Organization, and Expression Analysis of Zebrafish Nuclear Receptor Coactivator, TIF2.
  Zebrafish, 2, 33-46.  
15485860 C.Toleman, A.J.Paterson, T.R.Whisenhunt, and J.E.Kudlow (2004).
Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities.
  J Biol Chem, 279, 53665-53673.  
14536085 A.Clements, A.N.Poux, W.S.Lo, L.Pillus, S.L.Berger, and R.Marmorstein (2003).
Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase.
  Mol Cell, 12, 461-473.
PDB codes: 1pu9 1pua 1q2c
14661947 A.N.Poux, and R.Marmorstein (2003).
Molecular basis for Gcn5/PCAF histone acetyltransferase selectivity for histone and nonhistone substrates.
  Biochemistry, 42, 14366-14374.
PDB code: 1q2d
12592013 D.L.Burk, N.Ghuman, L.E.Wybenga-Groot, and A.M.Berghuis (2003).
X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members.
  Protein Sci, 12, 426-437.
PDB code: 1n71
14502267 K.Zhao, X.Chai, A.Clements, and R.Marmorstein (2003).
Structure and autoregulation of the yeast Hst2 homolog of Sir2.
  Nat Struct Biol, 10, 864-871.
PDB code: 1q14
12391296 A.N.Poux, M.Cebrat, C.M.Kim, P.A.Cole, and R.Marmorstein (2002).
Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor.
  Proc Natl Acad Sci U S A, 99, 14065-14070.
PDB code: 1m1d
12142402 C.A.White-Ziegler, A.M.Black, S.H.Eliades, S.Young, and K.Porter (2002).
The N-acetyltransferase RimJ responds to environmental stimuli to repress pap fimbrial transcription in Escherichia coli.
  J Bacteriol, 184, 4334-4342.  
11994311 M.R.Langer, C.J.Fry, C.L.Peterson, and J.M.Denu (2002).
Modulating acetyl-CoA binding in the GCN5 family of histone acetyltransferases.
  J Biol Chem, 277, 27337-27344.  
12161746 M.W.Vetting, S.S.Hegde, F.Javid-Majd, J.S.Blanchard, and S.L.Roderick (2002).
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.
  Nat Struct Biol, 9, 653-658.
PDB codes: 1m44 1m4d 1m4g 1m4i
12110674 N.Adachi, A.Kimura, and M.Horikoshi (2002).
A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3.
  J Biol Chem, 277, 35688-35695.  
  12176388 T.E.Benson, D.B.Prince, V.T.Mutchler, K.A.Curry, A.M.Ho, R.W.Sarver, J.C.Hagadorn, G.H.Choi, and R.L.Garlick (2002).
X-ray crystal structure of Staphylococcus aureus FemA.
  Structure, 10, 1107-1115.
PDB code: 1lrz
11997517 W.H.Ludlam, M.H.Taylor, K.G.Tanner, J.M.Denu, R.H.Goodman, and S.M.Smolik (2002).
The acetyltransferase activity of CBP is required for wingless activation and H4 acetylation in Drosophila melanogaster.
  Mol Cell Biol, 22, 3832-3841.  
12478591 Y.Kimura, S.Nakamori, and H.Takagi (2002).
Polymorphism of the MPR1 gene required for toxic proline analogue resistance in the Saccharomyces cerevisiae complex species.
  Yeast, 19, 1437-1445.  
11160883 A.Ahmad, N.Nagamatsu, H.Kouriki, Y.Takami, and T.Nakayama (2001).
Leucine zipper motif of chicken histone acetyltransferase-1 is essential for in vivo and in vitro interactions with the p48 subunit of chicken chromatin assembly factor-1.
  Nucleic Acids Res, 29, 629-637.  
11585814 A.M.Makowski, R.N.Dutnall, and A.T.Annunziato (2001).
Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase.
  J Biol Chem, 276, 43499-43502.  
11709299 A.Shmara, N.Weinsetel, K.J.Dery, R.Chavideh, and M.E.Tolmasky (2001).
Systematic analysis of a conserved region of the aminoglycoside 6'-N-acetyltransferase type Ib.
  Antimicrob Agents Chemother, 45, 3287-3292.  
11487463 G.V.Denis (2001).
Duality in bromodomain-containing protein complexes.
  Front Biosci, 6, D849-D852.  
11691934 L.Bordoli, S.Hüsser, U.Lüthi, M.Netsch, H.Osmani, and R.Eckner (2001).
Functional analysis of the p300 acetyltransferase domain: the PHD finger of p300 but not of CBP is dispensable for enzymatic activity.
  Nucleic Acids Res, 29, 4462-4471.  
11555637 M.Shichiri, C.Hoshikawa, S.Nakamori, and H.Takagi (2001).
A novel acetyltransferase found in Saccharomyces cerevisiae Sigma1278b that detoxifies a proline analogue, azetidine-2-carboxylic acid.
  J Biol Chem, 276, 41998-42002.  
  11250138 R.Marmorstein, and S.Y.Roth (2001).
Histone acetyltransferases: function, structure, and catalysis.
  Curr Opin Genet Dev, 11, 155-161.  
11527156 S.Chakraborty, V.Senyuk, and G.Nucifora (2001).
Genetic lesions and perturbation of chromatin architecture: a road to cell transformation.
  J Cell Biochem, 82, 310-325.  
11395403 S.Y.Roth, J.M.Denu, and C.D.Allis (2001).
Histone acetyltransferases.
  Annu Rev Biochem, 70, 81.  
11828432 T.A.Keating, D.E.Ehmann, R.M.Kohli, C.G.Marshall, J.W.Trauger, and C.T.Walsh (2001).
Chain termination steps in nonribosomal peptide synthetase assembly lines: directed acyl-S-enzyme breakdown in antibiotic and siderophore biosynthesis.
  Chembiochem, 2, 99.  
11258703 Y.Takei, M.Swietlik, A.Tanoue, G.Tsujimoto, T.Kouzarides, and R.Laskey (2001).
MCM3AP, a novel acetyltransferase that acetylates replication protein MCM3.
  EMBO Rep, 2, 119-123.  
10882077 A.Akhtar, and P.B.Becker (2000).
Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila.
  Mol Cell, 5, 367-375.  
10856249 B.O.Wittschieben, J.Fellows, W.Du, D.J.Stillman, and J.Q.Svejstrup (2000).
Overlapping roles for the histone acetyltransferase activities of SAGA and elongator in vivo.
  EMBO J, 19, 3060-3068.  
10839822 D.E.Sterner, and S.L.Berger (2000).
Acetylation of histones and transcription-related factors.
  Microbiol Mol Biol Rev, 64, 435-459.  
11080160 D.J.Owen, P.Ornaghi, J.C.Yang, N.Lowe, P.R.Evans, P.Ballario, D.Neuhaus, P.Filetici, and A.A.Travers (2000).
The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p.
  EMBO J, 19, 6141-6149.
PDB code: 1e6i
10940244 F.Dyda, D.C.Klein, and A.B.Hickman (2000).
GCN5-related N-acetyltransferases: a structural overview.
  Annu Rev Biophys Biomol Struct, 29, 81.  
10777580 G.Boehmelt, I.Fialka, G.Brothers, M.D.McGinley, S.D.Patterson, R.Mo, C.C.Hui, S.Chung, L.A.Huber, T.W.Mak, and N.N.Iscove (2000).
Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association.
  J Biol Chem, 275, 12821-12832.  
10823961 L.Ko, G.R.Cardona, and W.W.Chin (2000).
Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator.
  Proc Natl Acad Sci U S A, 97, 6212-6217.  
10882143 O.D.Lau, T.K.Kundu, R.E.Soccio, S.Ait-Si-Ali, E.M.Khalil, A.Vassilev, A.P.Wolffe, Y.Nakatani, R.G.Roeder, and P.A.Cole (2000).
HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF.
  Mol Cell, 5, 589-595.  
11114158 Q.Zhang, H.Yao, N.Vo, and R.H.Goodman (2000).
Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP.
  Proc Natl Acad Sci U S A, 97, 14323-14328.  
  10817755 S.John, L.Howe, S.T.Tafrov, P.A.Grant, R.Sternglanz, and J.L.Workman (2000).
The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAF(II)30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex.
  Genes Dev, 14, 1196-1208.  
10688640 S.K.Galasinski, T.N.Lively, A.Grebe De Barron, and J.A.Goodrich (2000).
Acetyl coenzyme A stimulates RNA polymerase II transcription and promoter binding by transcription factor IID in the absence of histones.
  Mol Cell Biol, 20, 1923-1930.  
11123906 T.A.Farazi, J.K.Manchester, and J.I.Gordon (2000).
Transient-state kinetic analysis of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase reveals that a step after chemical transformation is rate limiting.
  Biochemistry, 39, 15807-15816.  
10966108 T.Ikura, V.V.Ogryzko, M.Grigoriev, R.Groisman, J.Wang, M.Horikoshi, R.Scully, J.Qin, and Y.Nakatani (2000).
Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis.
  Cell, 102, 463-473.  
10677216 T.Lechner, A.Lusser, A.Pipal, G.Brosch, A.Loidl, M.Goralik-Schramel, R.Sendra, S.Wegener, J.D.Walton, and P.Loidl (2000).
RPD3-type histone deacetylases in maize embryos.
  Biochemistry, 39, 1683-1692.  
11106757 Y.Yan, N.A.Barlev, R.H.Haley, S.L.Berger, and R.Marmorstein (2000).
Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.
  Mol Cell, 6, 1195-1205.
PDB code: 1fy7
10024876 A.B.Hickman, D.C.Klein, and F.Dyda (1999).
Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism.
  Mol Cell, 3, 23-32.
PDB code: 1b6b
10319816 A.B.Hickman, M.A.Namboodiri, D.C.Klein, and F.Dyda (1999).
The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.
  Cell, 97, 361-369.
PDB code: 1cjw
9889114 A.Travers (1999).
Chromatin modification: how to put a HAT on the histones.
  Curr Biol, 9, R23-R25.  
10445034 B.O.Wittschieben, G.Otero, T.de Bizemont, J.Fellows, H.Erdjument-Bromage, R.Ohba, Y.Li, C.D.Allis, P.Tempst, and J.Q.Svejstrup (1999).
A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme.
  Mol Cell, 4, 123-128.  
10545125 B.Polevoda, J.Norbeck, H.Takakura, A.Blomberg, and F.Sherman (1999).
Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae.
  EMBO J, 18, 6155-6168.  
10508725 G.D.Wright (1999).
Aminoglycoside-modifying enzymes.
  Curr Opin Microbiol, 2, 499-503.  
10413469 J.Wittmeyer, L.Joss, and T.Formosa (1999).
Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha.
  Biochemistry, 38, 8961-8971.  
10373413 K.G.Tanner, R.C.Trievel, M.H.Kuo, R.M.Howard, S.L.Berger, C.D.Allis, R.Marmorstein, and J.M.Denu (1999).
Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator.
  J Biol Chem, 274, 18157-18160.  
  10378269 L.E.Wybenga-Groot, K.Draker, G.D.Wright, and A.M.Berghuis (1999).
Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold.
  Structure, 7, 497-507.
PDB code: 1b87
10430873 R.C.Trievel, J.R.Rojas, D.E.Sterner, R.N.Venkataramani, L.Wang, J.Zhou, C.D.Allis, S.L.Berger, and R.Marmorstein (1999).
Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
  Proc Natl Acad Sci U S A, 96, 8931-8936.
PDB code: 1ygh
10430845 R.Sternglanz, and H.Schindelin (1999).
Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases.
  Proc Natl Acad Sci U S A, 96, 8807-8808.  
10322138 S.Jacobson, and L.Pillus (1999).
Modifying chromatin and concepts of cancer.
  Curr Opin Genet Dev, 9, 175-184.  
10395565 S.L.Berger (1999).
Gene activation by histone and factor acetyltransferases.
  Curr Opin Cell Biol, 11, 336-341.  
10205156 T.Izard, and A.Geerlof (1999).
The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity.
  EMBO J, 18, 2021-2030.
PDB code: 1b6t
  10072350 T.Kouzarides (1999).
Histone acetylases and deacetylases in cell proliferation.
  Curr Opin Genet Dev, 9, 40-48.  
9867860 T.Mio, T.Yamada-Okabe, M.Arisawa, and H.Yamada-Okabe (1999).
Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis.
  J Biol Chem, 274, 424-429.  
10384314 R.N.Dutnall, S.T.Tafrov, R.Sternglanz, and V.Ramakrishnan (1998).
Structure of the yeast histone acetyltransferase Hat1: insights into substrate specificity and implications for the Gcn5-related N-acetyltransferase superfamily.
  Cold Spring Harb Symp Quant Biol, 63, 501-507.  
  9817851 Y.Modis, and R.Wierenga (1998).
Two crystal structures of N-acetyltransferases reveal a new fold for CoA-dependent enzymes.
  Structure, 6, 1345-1350.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.