 |
|
Title
|
|
1H and 15N assignments and secondary structure of the starch-binding domain of glucoamylase from Aspergillus niger.
|
|
|
Authors
|
|
A.J.Jacks,
K.Sorimachi,
M.F.Le Gal-Coëffet,
G.Williamson,
D.B.Archer,
M.P.Williamson.
|
|
|
Ref.
|
|
Eur J Biochem, 1995,
233,
568-578.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
1H and 15N NMR resonance assignments of the granular starch-binding domain (SBD)
of glucoamylase from Aspergillus niger have been made by multi-dimensional
homonuclear and heteronuclear NMR techniques. Secondary structure analysis based
on chemical shifts, 1H-1H NOEs, coupling constants and backbone amide exchange
data indicates the presence of a well-defined beta-sheet structure. This
consists of one parallel and five antiparallel pairs of beta-strands forming two
beta-sheets. Cis-trans isomerisation of proline residues and O-glycosylation of
threonine residues are observed and compared between the proteolytically derived
SBD fragment and the recombinant protein. Structural features of the SBD in
solution were compared to the X-ray crystal structure of a homologous domain of
cyclodextrin glycosyltransferase from Bacillus circulans. There are some
differences in the locations of the start and end of beta-strands but overall
the two structures are very similar. This study will form the basis for the
structure determination of the granular SBD and of its complexes.
|
|
|
|