{"refrec":{"BRefID":280896,"RR":"<b>De Vos, D.; Collins, T.; Nerinckx, W.; Savvides, S.N.; Claeyssens, M.; Gerday, C.; Feller, G.; Van Beeumen, J.</b> (2006). Oligosaccharide binding in family 8 glycosidases: Crystal structures of active-site mutants of the β-1,4-xylanase pXyl from <i>Pseudoaltermonas haloplanktis</i> TAH3a in complex with substrate and product. <i>Biochemistry (Wash.) 45(15)</i>: 4797-4807. <a href=\"https://dx.doi.org/10.1021/bi052193e\" target=\"_blank\">https://dx.doi.org/10.1021/bi052193e</a>","BEntID":272915,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Biochemistry (Wash.) 45(15)</i>: 4797-4807. <a href=\"https://dx.doi.org/10.1021/bi052193e\" target=\"_blank\">https://dx.doi.org/10.1021/bi052193e</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"De Vos, D.; Collins, T.; Nerinckx, W.; Savvides, S.N.; Claeyssens, M.; Gerday, C.; Feller, G.; Van Beeumen, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"De Vos, D. <i>et al.</i>","Englishabstract":"The structures of inactive mutants D144A and E78Q of the glycoside hydrolase family 8 (GH-8) endo-β-1,4-d-xylanase (pXyl) from the Antarctic bacterium <i>Pseudoalteromonas haloplanktis</i> TAH3a in complex with its substrate xylopentaose (at 1.95 Å resolution) and product xylotriose (at 1.9 Å resolution) have been determined by X-ray crystallography. A detailed comparative analysis of these with the apo-enzyme and with other GH-8 structures indicates an induced fit mechanism upon ligand binding whereby a number of conformational changes and, in particular, a repositioning of the proton donor into a more catalytically competent position occurs. This has also allowed for the description of protein−ligand interactions in this enzyme and for the demarcation of subsites −3 to +3. An in-depth analysis of each of these subsites gives an insight into the structure−function relationship of this enzyme and the basis of xylose/glucose discrimination in family 8 glycoside hydrolases. Furthermore, the structure of the −1/+1 subsite spanning complex reveals that the substrate is distorted from its ground state conformation. Indeed, structural analysis and in silico docking studies indicate that substrate hydrolysis in GH-8 members is preceded by a conformational change, away from the substrate ground-state chair conformation, to a pretransition state local minimum <sup>2</sup><i>S</i><sub>O</sub> conformation. 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