Journal:Acta Cryst D:S2059798318014900
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The enzymatic degradation of starch has a myriad industrial applications. However, the branched nature of the polysaccharides that compose it poses problems, as branches have to be accommodated within an active centre best suited to linear polysaccharides. Alpha-amylases are glycoside hydrolases that break the α-1,4 bonds in starch and related glycans. The present work provides a rare insight into branch-point acceptance in these industrial catalysts. | The enzymatic degradation of starch has a myriad industrial applications. However, the branched nature of the polysaccharides that compose it poses problems, as branches have to be accommodated within an active centre best suited to linear polysaccharides. Alpha-amylases are glycoside hydrolases that break the α-1,4 bonds in starch and related glycans. The present work provides a rare insight into branch-point acceptance in these industrial catalysts. | ||
| - | The complex of AliC with acarbose was solved by molecular replacement, with two molecules of AliC in the asymmetric unit, at a resolution of 2.1 Å . The fold, as expected, is a canonical three-domain arrangement with the A, B and C domains defined approximately as A, residues 4–104 and 210–397, B, residues 105–209, and C, residues 398–484. A classical | + | The complex of AliC with acarbose was solved by molecular replacement, with two molecules of AliC in the asymmetric unit, at a resolution of 2.1 Å . The fold, as expected, is a canonical three-domain arrangement with the A, B and C domains defined approximately as A, residues 4–104 and 210–397, B, residues 105–209, and C, residues 398–484. A classical Ca<sup>2+</sup>–Na<sup>+</sup>– Ca<sup>2+</sup> triad (Machius et al., 1998; Brzozowski et al., 2000) is found at the A/Bdomain interface. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:25, 21 November 2018
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