Biochemical and Biophysical Research Communications 2012-08-03

Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.

Kimiko Chaen, Junji Noguchi, Toshiro Omori, Yoshimitsu Kakuta, Makoto Kimura

Index: Biochem. Biophys. Res. Commun. 424(3) , 508-11, (2012)

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Abstract

Starch branching enzyme (SBE) catalyzes the cleavage of α-1,4-linkages and the subsequent transfer of α-1,4 glucan to form an α-1,6 branch point in amylopectin. We determined the crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose at a resolution of 2.2Å. Maltopentaose bound to a hydrophobic pocket formed by the N-terminal helix, carbohydrate-binding module 48 (CBM48), and α-amylase domain. In addition, glucose moieties could be observed at molecular surfaces on the N-terminal helix (α2) and CBM48. Amino acid residues involved in the carbohydrate bindings are highly conserved in other SBEs, suggesting their generally conserved role in substrate binding for SBEs.Copyright © 2012 Elsevier Inc. All rights reserved.

Related Compounds

  • Cellopentaose
  • Maltopentaose

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