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PDBsum entry 2uvf
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* Residue conservation analysis
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DOI no:
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J Mol Biol
368:1215-1222
(2007)
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PubMed id:
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The structural basis for exopolygalacturonase activity in a family 28 glycoside hydrolase.
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D.W.Abbott,
A.B.Boraston.
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ABSTRACT
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Family 28 glycoside hydrolases (polygalacturonases) are found in organisms
across the plant, fungal and bacterial kingdoms, where they are central to
diverse biological functions such as fruit ripening, biomass recycling and plant
pathogenesis. The structures of several polygalacturonases have been reported;
however, all of these enzymes utilize an endo-mode of digestion, which generates
a spectrum of oligosaccharide products with varying degrees of polymerization.
The structure of a complementary exo-acting polygalacturonase and an
accompanying explanation of the molecular determinants for its specialized
activity have been noticeably lacking. We present the structure of an
exopolygalacturonase from Yersinia enterocolitica, YeGH28 in a native form
(solved to 2.19 A resolution) and a digalacturonic acid product complex (solved
to 2.10 A resolution). The activity of YeGH28 is due to inserted stretches of
amino acid residues that transform the active site from the open-ended channel
observed in the endopolygalacturonases to a closed pocket that restricts the
enzyme to the exclusive attack of the non-reducing end of oligogalacturonide
substrates. In addition, YeGH28 possesses a fused FN3 domain with unknown
function, the first such structure described in pectin active enzymes.
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Selected figure(s)
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
368,
1215-1222)
copyright 2007.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.A.Mertens,
and
M.J.Bowman
(2011).
Expression and characterization of fifteen Rhizopus oryzae 99-880 polygalacturonase enzymes in Pichia pastoris.
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Curr Microbiol,
62,
1173-1178.
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J.T.Noel,
N.Arrach,
A.Alagely,
M.McClelland,
and
M.Teplitski
(2010).
Specific responses of Salmonella enterica to tomato varieties and fruit ripeness identified by in vivo expression technology.
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PLoS One,
5,
e12406.
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C.Creze,
S.Castang,
E.Derivery,
R.Haser,
N.Hugouvieux-Cotte-Pattat,
V.E.Shevchik,
and
P.Gouet
(2008).
The crystal structure of pectate lyase peli from soft rot pathogen Erwinia chrysanthemi in complex with its substrate.
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J Biol Chem,
283,
18260-18268.
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PDB codes:
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D.W.Abbott,
and
A.B.Boraston
(2008).
Structural biology of pectin degradation by Enterobacteriaceae.
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Microbiol Mol Biol Rev,
72,
301.
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P.B.Vordtriede,
and
M.D.Yoder
(2008).
Crystallization, X-ray diffraction analysis and preliminary structure determination of the polygalacturonase PehA from Agrobacterium vitis.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
645-647.
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Z.Xiao,
S.Wang,
H.Bergeron,
J.Zhang,
and
P.C.Lau
(2008).
A flax-retting endopolygalacturonase-encoding gene from Rhizopus oryzae.
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Antonie Van Leeuwenhoek,
94,
563-571.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
