7BVT
Crystal structure of cyclic alpha-maltosyl-1,6-maltose binding protein from Arthrobacter globiformis
Summary for 7BVT
| Entry DOI | 10.2210/pdb7bvt/pdb |
| Descriptor | Hypothetical sugar ABC-transporter sugar binding protein, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
| Functional Keywords | substrate-binding protein, abc transporter, sugar binding protein |
| Biological source | Arthrobacter globiformis |
| Total number of polymer chains | 1 |
| Total formula weight | 44999.61 |
| Authors | Kohno, M.,Arakawa, T.,Mori, T.,Nishimoto, T.,Fushinobu, S. (deposition date: 2020-04-11, release date: 2020-12-02, Last modification date: 2023-11-29) |
| Primary citation | Kohno, M.,Arakawa, T.,Sunagawa, N.,Mori, T.,Igarashi, K.,Nishimoto, T.,Fushinobu, S. Molecular analysis of cyclic alpha-maltosyl-(1→6)-maltose binding protein in the bacterial metabolic pathway. Plos One, 15:e0241912-e0241912, 2020 Cited by PubMed 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. PubMed: 33211750DOI: 10.1371/journal.pone.0241912 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.47 Å) |
Structure validation
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