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PDBsum entry 2w1n
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References listed in PDB file
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Key reference
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Title
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Portrait of an enzyme, A complete structural analysis of a multimodular {beta}-N-Acetylglucosaminidase from clostridium perfringens.
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Authors
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E.Ficko-Blean,
K.J.Gregg,
J.J.Adams,
J.H.Hehemann,
M.Czjzek,
S.P.Smith,
A.B.Boraston.
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Ref.
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J Biol Chem, 2009,
284,
9876-9884.
[DOI no: ]
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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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Common features of the extracellular carbohydrate-active virulence factors
involved in host-pathogen interactions are their large sizes and modular
complexities. This has made them recalcitrant to structural analysis, and
therefore our understanding of the significance of modularity in these important
proteins is lagging. Clostridium perfringens is a prevalent human pathogen that
harbors a wide array of large, extracellular carbohydrate-active enzymes and is
an excellent and relevant model system to approach this problem. Here we
describe the complete structure of C. perfringens GH84C (NagJ), a 1001-amino
acid multimodular homolog of the C. perfringens micro-toxin, which was
determined using a combination of small angle x-ray scattering and x-ray
crystallography. The resulting structure reveals unprecedented insight into how
catalysis, carbohydrate-specific adherence, and the formation of molecular
complexes with other enzymes via an ultra-tight protein-protein interaction are
spatially coordinated in an enzyme involved in a host-pathogen interaction.
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Figure 2.
Structures of GH84C catalytic module and GH84C-CBM32 as
determined using x-ray crystallography and SAXS. A and B show
the crystal structures of GH84C catalytic module and
GH84C-CBM32, respectively, in a ribbon representation. The arrow
in B shows the C terminus of the CBM. C shows the
GASBOR-generated SAXS envelope of GH84C-CBM32, whereas D shows
the modules of GH84C-CBM32 manually fit into the SAXS envelope.
E shows the model in D without the SAXS form. F shows the
unmodified x-ray crystal structure, shown in B, fit into the
SAXS-generated envelope. All of the structures are shown from
identical orientations. The N-terminal domain is pictured in
light blue, the catalytic TIM barrel is in orange, the helical
bundle is in pale green, and the CBM in red.
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Figure 4.
Structural features of the Coh-FN3 modular pair. A shows a
ribbon representation of the 1.8-Å crystal structure of
Coh-FN3. The Coh module is depicted in blue, and FN3 is shown in
black. B shows the surface representation of Coh-FN3 colored
according to electrostatic potential (red is negative, and blue
is positive). The basic patch of FN3 is circled and expanded to
show a patch of basic residues.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2009,
284,
9876-9884)
copyright 2009.
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