 |
PDBsum entry 2vn4
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Three-Dimensional structure of an intact glycoside hydrolase family 15 glucoamylase from hypocrea jecorina.
|
|
|
Authors
|
|
R.Bott,
M.Saldajeno,
W.Cuevas,
D.Ward,
M.Scheffers,
W.Aehle,
S.Karkehabadi,
M.Sandgren,
H.Hansson.
|
|
|
Ref.
|
|
Biochemistry, 2008,
47,
5746-5754.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The three-dimensional structure of a complete Hypocrea jecorina glucoamylase has
been determined at 1.8 A resolution. The presented structure model includes the
catalytic and starch binding domains and traces the course of the 37-residue
linker segment. While the structures of other fungal and yeast glucoamylase
catalytic and starch binding domains have been determined separately, this is
the first intact structure that allows visualization of the juxtaposition of the
starch binding domain relative to the catalytic domain. The detailed
interactions we see between the catalytic and starch binding domains are
confirmed in a second independent structure determination of the enzyme in a
second crystal form. This second structure model exhibits an identical
conformation compared to the first structure model, which suggests that the H.
jecorina glucoamylase structure we report is independent of crystal lattice
contact restraints and represents the three-dimensional structure found in
solution. The proposed starch binding regions for the starch binding domain are
aligned with the catalytic domain in the three-dimensional structure in a manner
that supports the hypothesis that the starch binding domain serves to target the
glucoamylase at sites where the starch granular matrix is disrupted and where
the enzyme might most effectively function.
|
|
|
|
|
|
|
