Structure of the Sulfolobus solfataricus alpha-glucosidase: Implications for domain conservation and substrate recognition in GH31
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The crystal structure of a-glucosidase MalA from Sulfolobus solfataricus has been determined at 2.5 Å resolution. It provides a structural model for enzymes representing the major specificity in glycoside hydrolase family 31 (GH31), including a-glucosidases from higher organisms, involved in glycogen degradation and glycoprotein processing. The structure of MalA shows clear differences from the only other structure known from GH31, a-xylosidase YicI. MalA and YicI share only 23% sequence identity. Although the two enzymes display a similar domain structure and both form hexamers, their structures differ significantly in quaternary organization: MalA is a dimer of trimers, YicI a trimer of dimers. MalA and YicI also differ in their substrate specificities, as shown by kinetic measurements on model chromogenic substrates. In addition, MalA has a clear preference for maltose (Glc-a1,4-Glc), whereas YicI prefers isoprimeverose (Xyl-a1,6-Glc). The structural origin of this difference occurs in the -1 subsite where MalA residues Asp251 and Trp284 could interact with OH6 of the substrate. The structure of MalA in complex with ß-octyl-glucopyranoside has been determined. It reveals Arg400, Asp87, Trp284, Met321 and Phe327 as invariant residues forming the +1 subsite in the GH31 a-glucosidases. Structural comparisons with other GH families suggest that the GH31 enzymes belong to clan GH-D.
|Journal||Journal of Molecular Biology|
|Publication status||Published - 2006|
Keywords: glycoside hydrolase; substrate specificity; a-glucosidase; a-xylosidase; crystal structure