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 β‐sheet structure. This consists of one parallel and five antiparallel pairs of β‐strands forming two β‐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 glyco‐syltransferase from Bacillus circulans. There are some differences in the locations of the start and end of β‐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.
| Original language | English |
|---|---|
| Pages (from-to) | 568-578 |
| Number of pages | 11 |
| Journal | European Journal of Biochemistry |
| Volume | 233 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1 Jan 1995 |
| Externally published | Yes |
Keywords
- Aspergillus niger
- glucoamylase 1
- NMR
- secondary structure
- starch‐binding domain
Cite this
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1H and 15N Assignments and Secondary Structure of the Starch‐Binding Domain of Glucoamylase from Aspergillus niger. / Jacks, Amanda J.; Sorimachi, Kay; Le Gal‐Coëffet, Marie‐Francoise ‐F; Williamson, Gary; Archer, David B.; Williamson, Michael P.
In: European Journal of Biochemistry, Vol. 233, No. 2, 01.01.1995, p. 568-578.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - 1H and 15N Assignments and Secondary Structure of the Starch‐Binding Domain of Glucoamylase from Aspergillus niger
AU - Jacks, Amanda J.
AU - Sorimachi, Kay
AU - Le Gal‐Coëffet, Marie‐Francoise ‐F
AU - Williamson, Gary
AU - Archer, David B.
AU - Williamson, Michael P.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - 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 β‐sheet structure. This consists of one parallel and five antiparallel pairs of β‐strands forming two β‐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 glyco‐syltransferase from Bacillus circulans. There are some differences in the locations of the start and end of β‐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.
AB - 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 β‐sheet structure. This consists of one parallel and five antiparallel pairs of β‐strands forming two β‐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 glyco‐syltransferase from Bacillus circulans. There are some differences in the locations of the start and end of β‐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.
KW - Aspergillus niger
KW - glucoamylase 1
KW - NMR
KW - secondary structure
KW - starch‐binding domain
UR - http://www.scopus.com/inward/record.url?scp=0028972748&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1995.568_2.x
DO - 10.1111/j.1432-1033.1995.568_2.x
M3 - Article
VL - 233
SP - 568
EP - 578
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 2
ER -