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PDBsum entry 1ukc
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* Residue conservation analysis
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DOI no:
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Structure
12:677-687
(2004)
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PubMed id:
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Aspergillus niger protein EstA defines a new class of fungal esterases within the alpha/beta hydrolase fold superfamily of proteins.
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Y.Bourne,
A.A.Hasper,
H.Chahinian,
M.Juin,
L.H.De Graaff,
P.Marchot.
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ABSTRACT
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From the fungus Aspergillus niger, we identified a new gene encoding protein
EstA, a member of the alpha/beta-hydrolase fold superfamily but of unknown
substrate specificity. EstA was overexpressed and its crystal structure was
solved by molecular replacement using a lipase-acetylcholinesterase chimera
template. The 2.1 A resolution structure of EstA reveals a canonical Ser/Glu/His
catalytic triad located in a small pocket at the bottom of a large
solvent-accessible, bowl-shaped cavity. Potential substrates selected by manual
docking procedures were assayed for EstA activity. Consistent with the pocket
geometry, preference for hydrolysis of short acyl/propyl chain substrates was
found. Identification of close homologs from the genome of other fungi, of which
some are broad host-range pathogens, defines EstA as the first member of a novel
class of fungal esterases within the superfamily. Hence the structure of EstA
constitutes a lead template in the design of new antifungal agents directed
toward its pathogenic homologs.
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Selected figure(s)
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Figure 4.
Figure 4. Chemical Structures of the Substrates Hydrolyzed
by EstAThe vinyl esters (left) and triacylglycerols (right)
differ by the length of the acyl chain, with R = CH[3]
(acetate/triacetin), CH[2]-CH[3] (proponiate/tripropionin), and
(CH[2])[2]-CH[3] (butyrate/tributyrin).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
677-687)
copyright 2004.
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Figure was
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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T.Koseki,
S.Fushinobu,
Ardiansyah,
H.Shirakawa,
and
M.Komai
(2009).
Occurrence, properties, and applications of feruloyl esterases.
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Appl Microbiol Biotechnol,
84,
803-810.
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A.R.Stricker,
R.L.Mach,
and
L.H.de Graaff
(2008).
Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei).
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Appl Microbiol Biotechnol,
78,
211-220.
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I.Benoit,
M.Asther,
Y.Bourne,
D.Navarro,
S.Canaan,
L.Lesage-Meessen,
M.Herweijer,
P.M.Coutinho,
M.Asther,
and
E.Record
(2007).
Gene overexpression and biochemical characterization of the biotechnologically relevant chlorogenic acid hydrolase from Aspergillus niger.
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Appl Environ Microbiol,
73,
5624-5632.
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B.M.Nair,
L.A.Joachimiak,
S.Chattopadhyay,
I.Montano,
and
J.L.Burns
(2005).
Conservation of a novel protein associated with an antibiotic efflux operon in Burkholderia cenocepacia.
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FEMS Microbiol Lett,
245,
337-344.
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H.Zorn,
H.Bouws,
M.Takenberg,
M.Nimtz,
R.Getzlaff,
D.E.Breithaupt,
and
R.G.Berger
(2005).
An extracellular carboxylesterase from the basidiomycete Pleurotus sapidus hydrolyses xanthophyll esters.
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Biol Chem,
386,
435-440.
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J.D.Schrag,
and
M.Cygler
(2004).
Defining substrate characteristics from 3D structure; perspective on EstA structure.
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Structure,
12,
521-522.
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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.
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