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PDBsum entry 1i1d
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structures of apo and complexed saccharomyces cerevisiae gna1 shed light on the catalytic mechanism of an amino-Sugar n-Acetyltransferase.
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Authors
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C.Peneff,
D.Mengin-Lecreulx,
Y.Bourne.
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Ref.
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J Biol Chem, 2001,
276,
16328-16334.
[DOI no: ]
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PubMed id
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Abstract
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The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for
antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase
(GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the
formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal
structures corresponding to the apo Saccharomyces cerevisiae GNA1, the
GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4,
1.3, and 1.8 A resolution, respectively. These structures not only reveal a
stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site
located at the dimer interface but also shed light on the catalytic machinery of
GNA1 at an atomic level. Hence, they broaden our understanding of structural
features required for GNAT activity, provide structural details for related
aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT
superfamily members to acquire various specificities.
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Figure 3.
Fig. 3. Schematic representation of the proposed GNA1
catalytic mechanism.
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Figure 5.
Fig. 5. Structural comparison of substrate binding sites
of AANAT , tGCN5, and GNA1. The molecular surfaces around the
active site of the AANAT-bisubstrate analog (A), the
tGCN5-CoA-H3peptide (B), and the GNA1-CoA-GlcNAc6P complex
structures (C) are viewed with a similar orientation. From top
to bottom, the serotonin-like moiety and the acetyl group are
shown in red, the H3 peptide backbone in yellow, with its
reactive Lys-14 side chain in orange, and GlcNAc6P in purple.
Structural divergences within the NH[2]- and COOH-terminal
regions are highlighted in dark blue and blue, respectively. The
 3- 4 insertion
loop unique to AANAT is shown in brown.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
16328-16334)
copyright 2001.
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