5b68 | pdb_00005b68

Crystal structure of apo amylomaltase from Corynebacterium glutamicum

spinqualitylabelsall models 5b68, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b68 is a 1 chain structure with sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: BTB, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8NNA7_CORGL Publication Abstract from PubMed 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. Crystal Structure of Amylomaltase from Corynebacterium glutamicum.,Joo S, Kim S, Seo H, Kim KJ J Agric Food Chem. 2016 Jul 20;64(28):5662-70. doi: 10.1021/acs.jafc.6b02296., Epub 2016 Jul 8. PMID:27366969 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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