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PDBsum entry 2iq7
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the endopolygalacturonase from the phytopathogenic fungus colletotrichum lupini and its interaction with polygalacturonase-Inhibiting proteins.
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Authors
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D.Bonivento,
D.Pontiggia,
A.D.Matteo,
J.Fernandez-Recio,
G.Salvi,
D.Tsernoglou,
F.Cervone,
G.D.Lorenzo,
L.Federici.
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Ref.
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Proteins, 2008,
70,
294-299.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. (A) Ribbon representation of CluPG1. A cross section
of the  -helix
is shown on the right panel; the color code indicates the
secondary structure elements in a representative coil. (B)
Structural superposition of CluPG1 with AnPGII and FmPG. The red
circle indicates an eight residues insertion in the structure of
FmPG that likely plays a role in the interaction of this enzyme
with PGIPs.
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Figure 2.
Figure 2. (A) CluPG1 enzyme kinetics and inhibition played by
PvPGIP2. The uninhibited enzyme is represented in squares;
triangles and circles represent the data obtained in the
presence of 4 and 8 nM PvPGIP2, respectively. Curves represent
the fits of experimental data with non-linear regression
analysis using the Michaelis-Menten equation. K[m] and V[max]
values are reported in the inset. A decrease in V[max] while
K[m] remains constant is indicative of noncompetitive
inhibition. (B) Optimal docking areas of CluPG1, AnPGII, and
FmPG. Surface residues with an ODA value lower than -2 kcal/mol
are colored in red, otherwise in blue. Black arrows mark the
position of the active sites. The putative interaction areas of
CluPG1 and AnPGII, located below the binding cleft, are almost
superimposable. Differently, FmPG shows two distinct patches on
opposite sides of the active site. A different PG-PGIP
interaction area for the latter enzyme with respect to CluPG1
and AnPGII is suggested, which accounts for the different modes
of inhibition observed. The view is  90°
anticlockwise rotated over the z-axis with respect to Figure 1.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
70,
294-299)
copyright 2008.
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