TY - JOUR
T1 - Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose
AU - Chaen, Kimiko
AU - Noguchi, Junji
AU - Omori, Toshiro
AU - Kakuta, Yoshimitsu
AU - Kimura, Makoto
N1 - Funding Information:
We thank the staff of Spring-8 and the Photon Factory for their assistance in collecting data. The synchrotron radiation experiments were performed at the BL38B1 of Spring-8 with the approval of the Japan Synchrotron Radiation Research Institute (JASRI) (Proposal No. 2007B1359 and 2007B1995 ), and Photon Factory. This study was supported in part by a grant from the Research for Promoting Technological Seeds program of Japan Science and Technology Agency (No. 15-020 ) and by a grant from the Iijima Kinen Foundation .
PY - 2012/8/3
Y1 - 2012/8/3
N2 - 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.
AB - 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.
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U2 - 10.1016/j.bbrc.2012.06.145
DO - 10.1016/j.bbrc.2012.06.145
M3 - Article
C2 - 22771800
AN - SCOPUS:84864758794
SN - 0006-291X
VL - 424
SP - 508
EP - 511
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -