7bvt

Crystal structure of cyclic alpha-maltosyl-1,6-maltose binding protein from Arthrobacter globiformis

spinqualitylabelsall models 7bvt, resolution 1.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bvt is a 1 chain structure with sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.47Å Ligands: GLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D2YYD8_ARTGO Publication Abstract from PubMed Cyclic alpha-maltosyl-(1-->6)-maltose (CMM) is a cyclic glucotetrasaccharide with alternating alpha-1,4 and alpha-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 A, 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 alpha-nigerosyl-(1-->6)-nigerose and cyclodextrins. These results indicate that A. globiformis has a unique metabolic pathway specialized for CMM. Molecular analysis of cyclic alpha-maltosyl-(1-->6)-maltose binding protein in the bacterial metabolic pathway.,Kohno M, Arakawa T, Sunagawa N, Mori T, Igarashi K, Nishimoto T, Fushinobu S PLoS One. 2020 Nov 19;15(11):e0241912. doi: 10.1371/journal.pone.0241912. , eCollection 2020. PMID:33211750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA