5B68: Crystal Structure Of Apo Amylomaltase From Corynebacterium Glutamicum

Amylomaltase is an essential enzyme in maltose utilization and maltodextrin metabolism, and it has been industrially used for the production of cyclodextrin and modification of starch. We determined the crystal structure of amylomaltase from Corynebacterium glutamicum (CgAM) at a resolution of 1.7 A. Although CgAM forms a dimer without NaCl, it exists as a monomer in physiological concentration of NaCl. CgAM is composed of N- and C-terminal domains, which can be further divided into two and four subdomains, respectively. It exhibits a unique structural feature at the functionally unknown N-domain and also shows two striking differences at the C-domain compared to other amylomaltases. These differences at extended edge of the substrate-binding site might affect substrate specificity for large cyclodextrin formation. The bis-tris methane and sulfate molecules bound at the substrate-binding site of our current structure mimic the binding of the hydroxyl groups of glucose bound at subsites -1 and -2, respectively.
PDB ID: 5B68Download
MMDB ID: 141481
PDB Deposition Date: 2016/5/25
Updated in MMDB: 2016/08
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 5B68: monomeric; determined by author
Molecular Components in 5B68
Label Count Molecule
Protein (1 molecule)
Molecule annotation
Chemicals (12 molecules)
* Click molecule labels to explore molecular sequence information.

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