Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway
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 globi...
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| Veröffentlicht in: | PloS one 2020-11, Vol.15 (11), p.e0241912-e0241912 |
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| creator | Kohno, Masaki Arakawa, Takatoshi Sunagawa, Naoki Mori, Tetsuya Igarashi, Kiyohiko Nishimoto, Tomoyuki Fushinobu, Shinya |
| description | 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. |
| doi_str_mv | 10.1371/journal.pone.0241912 |
| format | Article |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0241912</identifier><identifier>PMID: 33211750</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Arthrobacter ; Arthrobacter - metabolism ; Binding sites ; Biology and Life Sciences ; Biotechnology ; Calorimetry ; Carbohydrates ; Chromatography ; Collaboration ; Crystal structure ; Crystallography, X-Ray ; Cyclodextrin ; Cyclodextrins ; Cyclodextrins - metabolism ; Disaccharides - metabolism ; Enzymes ; Glucose ; Gram-positive bacteria ; Ligands ; Maltose ; Maltose-binding protein ; Maltose-Binding Proteins - chemistry ; Maltose-Binding Proteins - metabolism ; Metabolic Networks and Pathways ; Metabolic pathways ; Metabolism ; Models, Molecular ; Molecular weight ; Physical Sciences ; Protein Conformation ; Protein Domains ; Proteins ; R&D ; Research & development ; Research and Analysis Methods ; Structure-function relationships ; Substrates ; Titration ; Titration calorimetry</subject><ispartof>PloS one, 2020-11, Vol.15 (11), p.e0241912-e0241912</ispartof><rights>2020 Kohno et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 Kohno et al 2020 Kohno et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-6b779f25d0062f24d58b54a0eb7d31668df1b3d23d70514e0bf81082b61789013</citedby><cites>FETCH-LOGICAL-c526t-6b779f25d0062f24d58b54a0eb7d31668df1b3d23d70514e0bf81082b61789013</cites><orcidid>0000-0001-6496-5440 ; 0000-0003-1346-6435</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7676653/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7676653/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33211750$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kohno, Masaki</creatorcontrib><creatorcontrib>Arakawa, Takatoshi</creatorcontrib><creatorcontrib>Sunagawa, Naoki</creatorcontrib><creatorcontrib>Mori, Tetsuya</creatorcontrib><creatorcontrib>Igarashi, Kiyohiko</creatorcontrib><creatorcontrib>Nishimoto, Tomoyuki</creatorcontrib><creatorcontrib>Fushinobu, Shinya</creatorcontrib><title>Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>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.</description><subject>Arthrobacter</subject><subject>Arthrobacter - metabolism</subject><subject>Binding sites</subject><subject>Biology and Life Sciences</subject><subject>Biotechnology</subject><subject>Calorimetry</subject><subject>Carbohydrates</subject><subject>Chromatography</subject><subject>Collaboration</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Cyclodextrin</subject><subject>Cyclodextrins</subject><subject>Cyclodextrins - metabolism</subject><subject>Disaccharides - metabolism</subject><subject>Enzymes</subject><subject>Glucose</subject><subject>Gram-positive bacteria</subject><subject>Ligands</subject><subject>Maltose</subject><subject>Maltose-binding protein</subject><subject>Maltose-Binding Proteins - chemistry</subject><subject>Maltose-Binding Proteins - metabolism</subject><subject>Metabolic Networks and 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Takatoshi</au><au>Sunagawa, Naoki</au><au>Mori, Tetsuya</au><au>Igarashi, Kiyohiko</au><au>Nishimoto, Tomoyuki</au><au>Fushinobu, Shinya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2020-11-19</date><risdate>2020</risdate><volume>15</volume><issue>11</issue><spage>e0241912</spage><epage>e0241912</epage><pages>e0241912-e0241912</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>33211750</pmid><doi>10.1371/journal.pone.0241912</doi><orcidid>https://orcid.org/0000-0001-6496-5440</orcidid><orcidid>https://orcid.org/0000-0003-1346-6435</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Arthrobacter Arthrobacter - metabolism Binding sites Biology and Life Sciences Biotechnology Calorimetry Carbohydrates Chromatography Collaboration Crystal structure Crystallography, X-Ray Cyclodextrin Cyclodextrins Cyclodextrins - metabolism Disaccharides - metabolism Enzymes Glucose Gram-positive bacteria Ligands Maltose Maltose-binding protein Maltose-Binding Proteins - chemistry Maltose-Binding Proteins - metabolism Metabolic Networks and Pathways Metabolic pathways Metabolism Models, Molecular Molecular weight Physical Sciences Protein Conformation Protein Domains Proteins R&D Research & development Research and Analysis Methods Structure-function relationships Substrates Titration Titration calorimetry |
| title | Molecular analysis of cyclic α-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway |
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