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PDBsum entry 2hhc
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References listed in PDB file
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Key reference
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Title
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High-Resolution structure of nodz fucosyltransferase involved in the biosynthesis of the nodulation factor.
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Authors
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K.Brzezinski,
T.Stepkowski,
S.Panjikar,
G.Bujacz,
M.Jaskolski.
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Ref.
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Acta Biochim Pol, 2007,
54,
537-549.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The fucosyltransferase NodZ is involved in the biosynthesis of the nodulation
factor in nitrogen-fixing symbiotic bacteria. It catalyzes alpha1,6 transfer of
l-fucose from GDP-fucose to the reducing residue of the synthesized Nod
oligosaccharide. We present the structure of the NodZ protein from
Bradyrhizobium expressed in Escherichia coli and crystallized in the presence of
phosphate ions in two crystal forms. The enzyme is arranged into two domains of
nearly equal size. Although NodZ falls in one broad class (GT-B) with other
two-domain glycosyltransferases, the topology of its domains deviates from the
canonical Rossmann fold, with particularly high distortions in the N-terminal
domain. Mutational data combined with structural and sequence alignments
indicate residues of potential importance in GDP-fucose binding or in the
catalytic mechanism. They are all clustered in three conserved sequence motifs
located in the C-terminal domain.
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Secondary reference #1
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Title
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Cloning, Purification, Crystallization and preliminary crystallographic studies of bradyrhizobium fucosyltransferase nodz.
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Authors
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K.Brzezinski,
B.Rogozinski,
T.Stepkowski,
G.Bujacz,
M.Jaskolski.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2004,
60,
344-346.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 A single crystal of native  -1,6-fucosyltransferase
NodZ (approximate dimensions 0.05 × 0.05 × 0.3 mm).
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Rhizobium sp. Strain ngr234 nodz protein is a fucosyltransferase.
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Authors
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D.Quesada-Vincens,
R.Fellay,
T.Nasim,
V.Viprey,
U.Burger,
J.C.Prome,
W.J.Broughton,
S.Jabbouri.
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Ref.
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J Bacteriol, 1997,
179,
5087-5093.
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PubMed id
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Secondary reference #3
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Title
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Bacterial nodulation protein nodz is a chitin oligosaccharide fucosyltransferase which can also recognize related substrates of animal origin.
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Authors
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C.Quinto,
A.H.Wijfjes,
G.V.Bloemberg,
L.Blok-Tip,
I.M.López-Lara,
B.J.Lugtenberg,
J.E.Thomas-Oates,
H.P.Spaink.
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Ref.
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Proc Natl Acad Sci U S A, 1997,
94,
4336-4341.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Construction of plasmids.
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Figure 3.
Fig. 3. TLC analysis of reaction products of NodZ protein
with various substrates and GDP-  -L-[U-^14C]fucose.
(A) Silica TLC. Lanes: 1, standard GDP- -L-[U-^14C]fucose;
2, incubation of the negative control extract shown^ in Fig. 2A,
lane 2, with chitin pentasaccharide; 3, chitin
hexasaccharide;^ 4, chitin pentasaccharide; 5, chitin
tetrasaccharide; 6, chitin^ trisaccharide; 7, chitin
disaccharide; 8, N-acetylglucosamine;^ and 9, standard
radiolabeled chitin oligosaccharides (chain-length^ V to II) and
N-acetylglucosamine (I) as described by Kamst et^ al. (3).
Indicated at the left is the migration of the reference^
compounds L-fucose and L-fucose 1-phosphate. (B) C[18]-silica
TLC.^ Lanes: 1, LCO NodRlv-V (C18:4, Ac); 2, mixture of LCOs
NodRlv-IV;^ 3, standard of nonfucosylated ^14C-labeled LCOs
NodRlv-V and NodRlv-IV (ref. 19; nomenclature^ described in ref.
12). (C) Silica TLC.
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