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PDBsum entry 2jzc
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References listed in PDB file
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Key reference
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Title
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Solution structure of alg13: the sugar donor subunit of a yeast n-Acetylglucosamine transferase.
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Authors
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X.Wang,
T.Weldeghiorghis,
G.Zhang,
B.Imperiali,
J.H.Prestegard.
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Ref.
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Structure, 2008,
16,
965-975.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of Alg13, the glycosyl donor-binding domain of an
important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae,
is presented. This glycosyltransferase is unusual in that it is active only in
the presence of a binding partner, Alg14. Alg13 is found to adopt a unique
topology among glycosyltransferases. Rather than the conventional Rossmann fold
found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like
fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the
C-terminal half of Alg13 is conserved. However, although conventional GT-B
enzymes usually possess three helices at the C terminus, only two helices are
present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl
donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13
with the sugar donor is primarily through the residues in the C-terminal half of
the protein.
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Figure 2.
Figure 2. Annotated HSQC Spectrum of Deuterated Alg13
Each assigned peak is labeled with the residue number and one
letter residue name.
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Figure 4.
Figure 4. Topology Representations of Alg 13
(A)
Schematic illustration of the predicted topology of Alg13. The
numbering of the element is according to the scheme from Figure
1. Note that the predicted helix after β2 gave rise to both α3
and β3.
(B) Schematic illustration of the experimentally
determined topology of Alg13.
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The above figures are
reprinted
from an Open Access publication published by Cell Press:
Structure
(2008,
16,
965-975)
copyright 2008.
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