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Crystal structures of starch binding domain from Rhizopus oryzae glucoamylase in complex with isomaltooligosaccharide: Insights into polysaccharide binding mechanism of CBM21 family

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0134(199711)29:3<334::aid-prot7>3.0.co;2-aopenalex-snapshot

Glucoamylase structural, functional, and evolutionary relationships

inferredcites →https://doi.org/10.1016/j.jcs.2003.12.001openalex-snapshot

Starch—composition, fine structure and architecture

inferredcites →https://doi.org/10.1016/j.jmb.2006.03.058openalex-snapshot

Crystal Structure of Pullulanase: Evidence for Parallel Binding of Oligosaccharides in the Active Site

inferredcites →https://doi.org/10.1016/j.jmb.2006.10.018openalex-snapshot

The Structural Basis of α-Glucan Recognition by a Family 41 Carbohydrate-binding Module from Thermotoga maritima

inferredcites →https://doi.org/10.1016/s0014-5793(99)00263-xopenalex-snapshot

The starch‐binding domain from glucoamylase disrupts the structure of starch

inferredcites →https://doi.org/10.1016/s0076-6879(97)76066-xopenalex-snapshot

[20] Processing of X-ray diffraction data collected in oscillation mode

inferredcites →https://doi.org/10.1016/s0096-5332(08)60122-8openalex-snapshot

Aspects of the Physical Chemistry of Starch

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Aromatic Stacking in the Sugar Binding Site of the Lactose Permease

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Importance of Hydrophobic and Polar Residues in Ligand Binding in the Family 15 Carbohydrate-Binding Module from Cellvibrio japonicus Xyn10C

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Three-Dimensional Structure of an Intact Glycoside Hydrolase Family 15 Glucoamylase from Hypocrea jecorina

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Trp22, Trp24, and Tyr8 Play a Pivotal Role in the Binding of the Family 10 Cellulose-Binding Module from Pseudomonas Xylanase A to Insoluble Ligands+

inferredcites →https://doi.org/10.1042/bj20040892openalex-snapshot

Carbohydrate-binding modules: fine-tuning polysaccharide recognition

inferredcites →https://doi.org/10.1042/bj20051982openalex-snapshot

The family 21 carbohydrate-binding module of glucoamylase from Rhizopus oryzae consists of two sites playing distinct roles in ligand binding

inferredcites →https://doi.org/10.1042/bj20061312openalex-snapshot

Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase

inferredcites →https://doi.org/10.1042/bj20080580openalex-snapshot

Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path

inferredcites →https://doi.org/10.1042/bj2800309openalex-snapshot

A classification of glycosyl hydrolases based on amino acid sequence similarities

inferredcites →https://doi.org/10.1093/bioinformatics/btq084openalex-snapshot

Feature-incorporated alignment based ligand-binding residue prediction for carbohydrate-binding modules

inferredcites →https://doi.org/10.1093/nar/gkn663openalex-snapshot

The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics

inferredcites →https://doi.org/10.1104/pp.107.3.673openalex-snapshot

What Controls the Amount and Structure of Starch in Storage Organs?

inferredcites →https://doi.org/10.1107/s0021889897006766openalex-snapshot

MOLREP : an Automated Program for Molecular Replacement

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Coot : model-building tools for molecular graphics

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REFMAC 5 dictionary: organization of prior chemical knowledge and guidelines for its use

inferredcites →https://doi.org/10.1107/s090744490705024xopenalex-snapshot

Iterative model building, structure refinement and density modification with thePHENIX AutoBuildwizard

inferredcites →https://doi.org/10.1271/bbb.61.1233openalex-snapshot

Molecular Mechanism inα-Glucosidase and Glucoamylase

inferredcites →https://doi.org/10.1371/journal.pone.0024814openalex-snapshot

Hydrophilic Aromatic Residue and in silico Structure for Carbohydrate Binding Module

inferredcites →https://doi.org/10.1371/journal.pone.0041131openalex-snapshot

Two Unique Ligand-Binding Clamps of Rhizopus oryzae Starch Binding Domain for Helical Structure Disruption of Amylose

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