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PDBsum entry 1ro7
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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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Structural analysis of the sialyltransferase cstii from campylobacter jejuni in complex with a substrate analog.
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Authors
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C.P.Chiu,
A.G.Watts,
L.L.Lairson,
M.Gilbert,
D.Lim,
W.W.Wakarchuk,
S.G.Withers,
N.C.Strynadka.
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Ref.
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Nat Struct Mol Biol, 2004,
11,
163-170.
[DOI no: ]
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PubMed id
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Abstract
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Sialic acid terminates oligosaccharide chains on mammalian and microbial cell
surfaces, playing critical roles in recognition and adherence. The enzymes that
transfer the sialic acid moiety from cytidine-5'-monophospho-N-acetyl-neuraminic
acid (CMP-NeuAc) to the terminal positions of these key glycoconjugates are
known as sialyltransferases. Despite their important biological roles, little is
understood about the mechanism or molecular structure of these
membrane-associated enzymes. We report the first structure of a
sialyltransferase, that of CstII from Campylobacter jejuni, a highly prevalent
foodborne pathogen. Our structural, mutagenesis and kinetic data provide support
for a novel mode of substrate binding and glycosyl transfer mechanism, including
essential roles of a histidine (general base) and two tyrosine residues
(coordination of the phosphate leaving group). This work provides a framework
for understanding the activity of several sialyltransferases, from bacterial to
human, and for the structure-based design of specific inhibitors.
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Figure 1.
Figure 1. Reaction scheme of CstII. The bond created in the
monofunctional and binfunctional reaction is highlighted by a
green circle.
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Figure 2.
Figure 2. The overall architecture of CstII  32.
(a) Arrangement of the CstII  32
tetramer. Each monomer is colored differentially. CMP-3FNeuAc is
shown as a stick representation in a magenta color, indicating
the location of the catalytic center. (b) View of CstII 32
monomer showing the N-terminal domain and the lid domain with
bound donor sugar analog. CMP-3FNeuAc is depicted in a red stick
representation. The N terminus, C terminus, individual strands
and individual helices are labeled.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
163-170)
copyright 2004.
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