Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin (Q27739645)

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G Williamson

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D B Archer

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M P Williamson

Regional distant sequence homology between amylases, alpha-glucosidases and transglucanosylases.

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publication date

15 May 1997

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published in

Structure

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volume

5

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issue

5

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page(s)

647-61

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cites work

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Nucleotide sequence of the raw-starch-digesting amylase gene from sp. B1018 and its strong homology to the cyclodextrin glucanotransferase genes

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Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form

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Structure of the gene encoding the exoglucanase of Cellulomonas fimi

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Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing

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Solution structure of a cellulose-binding domain from Cellulomonas fimi by nuclear magnetic resonance spectroscopy

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Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy

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Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution

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Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy

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1H and 15N Assignments and Secondary Structure of the Starch‐Binding Domain of Glucoamylase from Aspergillus niger

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Expression in Aspergillus niger of the starch-binding domain of glucoamylase. Comparison with the proteolytically produced starch-binding domain

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The 2.0-A resolution structure of soybean beta-amylase complexed with alpha-cyclodextrin

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Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9195884

1 reference

Consolidated OpenCitations Corpus – April 2017