6se9

Cold-adapted beta-D-galactosidase from Arthrobacter sp. 32cB mutant E441Q in complex with lactose bound in shallow mode

spinqualitylabelsall models 6se9, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6se9 is a 1 chain structure with sequence from Arthrobacter sp. 32cB. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.965Å Ligands: ACT, BGC, FMT, FRU, GAL, MLI, NA, PRD_900004 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A023UGN9_9MICC Publication Abstract from PubMed ArthbetaDG is a dimeric, cold-adapted beta-d-galactosidase that exhibits high hydrolytic and transglycosylation activity. A series of crystal structures of its wild form, as well as its ArthbetaDG_E441Q mutein complexes with ligands were obtained in order to describe the mode of its action. The ArthbetaDG_E441Q mutein is an inactive form of the enzyme designed to enable observation of enzyme interaction with its substrate. The resulting three-dimensional structures of complexes: ArthbetaDG_E441Q/LACs and ArthbetaDG/IPTG (ligand bound in shallow mode) and structures of complexes ArthbetaDG_E441Q/LACd, ArthbetaDG/ONPG (ligands bound in deep mode), and galactose ArthbetaDG/GAL and their analysis enabled structural characterization of the hydrolysis reaction mechanism. Furthermore, comparative analysis with mesophilic analogs revealed the most striking differences in catalysis mechanisms. The key role in substrate transfer from shallow to deep binding mode involves rotation of the F581 side chain. It is worth noting that the 10-aa loop restricting access to the active site in mesophilic GH2 betaDGs, in ArthbetaDG is moved outward. This facilitates access of substrate to active site. Such a permanent exposure of the entrance to the active site may be a key factor for improved turnover rate of the cold adapted enzyme and thus a structural feature related to its cold adaptation. Active Site Architecture and Reaction Mechanism Determination of Cold Adapted beta-d-galactosidase from Arthrobacter sp. 32cB.,Rutkiewicz M, Bujacz A, Wanarska M, Wierzbicka-Wos A, Cieslinski H Int J Mol Sci. 2019 Sep 3;20(17). pii: ijms20174301. doi: 10.3390/ijms20174301. PMID:31484304 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase 3D structures

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