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PDBsum entry 6cw2
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Gene regulation
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PDB id
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6cw2
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Contents |
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241 a.a.
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115 a.a.
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217 a.a.
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199 a.a.
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PDB id:
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Gene regulation
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Title:
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Crystal structure of a yeast saga transcriptional coactivator ada2/gcn5 hat subcomplex, crystal form 1
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Structure:
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Histone acetyltransferase gcn5. Chain: d. Engineered: yes. Transcriptional adapter 2. Chain: c. Engineered: yes. Antibody heavy chain. Chain: a. Engineered: yes.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: gcn5, ada4, swi9, ygr252w. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Organism_taxid: 4932. Gene: ada2, sckg_0090.
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Resolution:
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2.67Å
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R-factor:
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0.252
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R-free:
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0.284
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Authors:
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J.Sun,M.Paduch,S.A.Kim,R.M.Kramer,A.F.Barrios,V.Lu,J.Luke,S.Usatyuk, A.A.Kossiakoff,S.Tan
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Key ref:
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J.Sun
et al.
(2018).
Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.
Proc Natl Acad Sci U S A,
115,
10010-10015.
PubMed id:
DOI:
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Date:
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29-Mar-18
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Release date:
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19-Sep-18
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PROCHECK
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Headers
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References
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Q03330
(GCN5_YEAST) -
Histone acetyltransferase GCN5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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439 a.a.
241 a.a.
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Q02336
(ADA2_YEAST) -
Transcriptional adapter 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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434 a.a.
115 a.a.
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Enzyme class 2:
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Chain D:
E.C.2.3.1.-
- ?????
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Enzyme class 3:
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Chain D:
E.C.2.3.1.48
- histone acetyltransferase.
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Reaction:
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L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
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L-lysyl-[protein]
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+
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acetyl-CoA
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=
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N(6)-acetyl-L-lysyl-[protein]
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+
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CoA
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Proc Natl Acad Sci U S A
115:10010-10015
(2018)
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PubMed id:
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Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.
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J.Sun,
M.Paduch,
S.A.Kim,
R.M.Kramer,
A.F.Barrios,
V.Lu,
J.Luke,
S.Usatyuk,
A.A.Kossiakoff,
S.Tan.
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ABSTRACT
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The Gcn5 histone acetyltransferase (HAT) subunit of the SAGA transcriptional
coactivator complex catalyzes acetylation of histone H3 and H2B N-terminal
tails, posttranslational modifications associated with gene activation. Binding
of the SAGA subunit partner Ada2 to Gcn5 activates Gcn5's intrinsically weak HAT
activity on histone proteins, but the mechanism for this activation by the Ada2
SANT domain has remained elusive. We have employed Fab antibody fragments as
crystallization chaperones to determine crystal structures of a yeast Ada2/Gcn5
complex. Our structural and biochemical results indicate that the Ada2 SANT
domain does not activate Gcn5's activity by directly affecting histone peptide
binding as previously proposed. Instead, the Ada2 SANT domain enhances Gcn5
binding of the enzymatic cosubstrate acetyl-CoA. This finding suggests a
mechanism for regulating chromatin modification enzyme activity: controlling
binding of the modification cosubstrate instead of the histone substrate.
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