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

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

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25 Citations (Scopus)

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 2.2 å. 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.

Original languageEnglish
Pages (from-to)508-511
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume424
Issue number3
DOIs
Publication statusPublished - Aug 3 2012

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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