TY - JOUR
T1 - Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway
AU - Kohno, Masaki
AU - Arakawa, Takatoshi
AU - Sunagawa, Naoki
AU - Mori, Tetsuya
AU - Igarashi, Kiyohiko
AU - Nishimoto, Tomoyuki
AU - Fushinobu, Shinya
N1 - Funding Information:
This study was partially supported by JSPS-KAKENHI (15H02443, 26660083, and 24380053 to S. F.; and 15H04526, 18H02252 and 19H03013 to K. I.), a Grant-in-Aid for Innovative Areas from the Japanese Ministry of Education, Culture, Sports, and Technology (MEXT) (No. 18H05494 to K.I.), and Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)) from the Japanese Ministry of Education, Culture, Sports, and Technology (MEXT). Hayashibara Co. Ltd. provided support in the form of salaries three authors (MK, TM,TN), but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. The specific roles of these authors are articulated in the ?author contributions? section. We thank the staff at the Photon Factory and SPring-8 for the X-ray data collection, Professor Masahiro Samejima for helpful assistance with the ITC measurements, and Dr. Chihaya Yamada for technical assistance.
Publisher Copyright:
© 2020 Kohno et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2020/11
Y1 - 2020/11
N2 - Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC importer system of the bacteria Arthrobacter globiformis. Isothermal titration calorimetry analysis revealed that CMMBP specifically bound to CMM with a Kd value of 9.6 nM. The crystal structure of CMMBP was determined at a resolution of 1.47 Å, and a panose molecule was bound in a cleft between two domains. To delineate its structural features, the crystal structure of CMMBP was compared with other SBPs specific for carbohydrates, such as cyclic α-nigerosyl-(1→6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.
AB - Cyclic α-maltosyl-(1→6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating α-1,4 and α-1,6 linkages. Here, we report functional and structural analyses on CMM-binding protein (CMMBP), which is a substrate-binding protein (SBP) of an ABC importer system of the bacteria Arthrobacter globiformis. Isothermal titration calorimetry analysis revealed that CMMBP specifically bound to CMM with a Kd value of 9.6 nM. The crystal structure of CMMBP was determined at a resolution of 1.47 Å, and a panose molecule was bound in a cleft between two domains. To delineate its structural features, the crystal structure of CMMBP was compared with other SBPs specific for carbohydrates, such as cyclic α-nigerosyl-(1→6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM.
UR - http://www.scopus.com/inward/record.url?scp=85096458630&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0241912
DO - 10.1371/journal.pone.0241912
M3 - Article
C2 - 33211750
VL - 15
SP - e0241912
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 11
M1 - e0241912
ER -