4mdp | pdb_00004mdp

Crystal structure of a GH1 beta-glucosidase from the fungus Humicola insolens in complex with glucose

spinqualitylabelsall models 4mdp, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mdp is a 1 chain structure with sequence from Humicola grisea var. thermoidea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, GOL, PEG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O93784_HUMGT Publication Abstract from PubMed Product inhibition of beta-glucosidases (BGs) by glucose is considered to be a limiting step in enzymatic technologies for plant-biomass saccharification. Remarkably, some beta-glucosidases belonging to the GH1 family exhibit unusual properties, being tolerant to, or even stimulated by, high glucose concentrations. However, the structural basis for the glucose tolerance and stimulation of BGs is still elusive. To address this issue, the first crystal structure of a fungal beta-glucosidase stimulated by glucose was solved in native and glucose-complexed forms, revealing that the shape and electrostatic properties of the entrance to the active site, including the +2 subsite, determine glucose tolerance. The aromatic Trp168 and the aliphatic Leu173 are conserved in glucose-tolerant GH1 enzymes and contribute to relieving enzyme inhibition by imposing constraints at the +2 subsite that limit the access of glucose to the -1 subsite. The GH1 family beta-glucosidases are tenfold to 1000-fold more glucose tolerant than GH3 BGs, and comparative structural analysis shows a clear correlation between active-site accessibility and glucose tolerance. The active site of GH1 BGs is located in a deep and narrow cavity, which is in contrast to the shallow pocket in the GH3 family BGs. These findings shed light on the molecular basis for glucose tolerance and indicate that GH1 BGs are more suitable than GH3 BGs for biotechnological applications involving plant cell-wall saccharification. Structural basis for glucose tolerance in GH1 beta-glucosidases.,de Giuseppe PO, Souza Tde A, Souza FH, Zanphorlin LM, Machado CB, Ward RJ, Jorge JA, Furriel Rdos P, Murakami MT Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1631-9. doi:, 10.1107/S1399004714006920. Epub 2014 May 24. PMID:24914974 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-glucosidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA