Matches in SemOpenAlex for { <https://semopenalex.org/work/W2083354414> ?p ?o ?g. }
- W2083354414 endingPage "1124" @default.
- W2083354414 startingPage "1106" @default.
- W2083354414 abstract "The crystal structure of alpha-glucosidase MalA from Sulfolobus solfataricus has been determined at 2.5Angstrom resolution. It provides a structural model for enzymes representing the major specificity in glycoside hydrolase family 31 (GH31), including alpha-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, alpha-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-alpha1,4-Glc), whereas YicI prefers isoprimeverose (Xyl-alpha1,6-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 beta-octyl-glucopyranoside has been determined. It reveals Arg400, Asp87, Trp284, Met321 and Phe327 as invariant residues forming the +1 subsite in the GH31 alpha-glucosidases. Structural comparisons with other GH families suggest that the GH31 enzymes belong to clan GH-D." @default.
- W2083354414 created "2016-06-24" @default.
- W2083354414 creator A5014552647 @default.
- W2083354414 creator A5020399284 @default.
- W2083354414 creator A5027060726 @default.
- W2083354414 creator A5028789665 @default.
- W2083354414 creator A5042010650 @default.
- W2083354414 creator A5078105743 @default.
- W2083354414 date "2006-05-01" @default.
- W2083354414 modified "2023-09-29" @default.
- W2083354414 title "Structure of the Sulfolobus solfataricus α-Glucosidase: Implications for Domain Conservation and Substrate Recognition in GH31" @default.
- W2083354414 cites W1534369816 @default.
- W2083354414 cites W1548179157 @default.
- W2083354414 cites W1556656519 @default.
- W2083354414 cites W1562852007 @default.
- W2083354414 cites W1590476964 @default.
- W2083354414 cites W1624669825 @default.
- W2083354414 cites W1772341111 @default.
- W2083354414 cites W1856872680 @default.
- W2083354414 cites W1935712031 @default.
- W2083354414 cites W1964186790 @default.
- W2083354414 cites W1972960295 @default.
- W2083354414 cites W1974547091 @default.
- W2083354414 cites W1977709772 @default.
- W2083354414 cites W1978096114 @default.
- W2083354414 cites W1991213853 @default.
- W2083354414 cites W1995017064 @default.
- W2083354414 cites W1997739855 @default.
- W2083354414 cites W2000840258 @default.
- W2083354414 cites W2001573278 @default.
- W2083354414 cites W2001838494 @default.
- W2083354414 cites W2011845231 @default.
- W2083354414 cites W2013083986 @default.
- W2083354414 cites W2014834146 @default.
- W2083354414 cites W2018866047 @default.
- W2083354414 cites W2022058405 @default.
- W2083354414 cites W2028231353 @default.
- W2083354414 cites W2031357907 @default.
- W2083354414 cites W2031772330 @default.
- W2083354414 cites W2037891557 @default.
- W2083354414 cites W2039018023 @default.
- W2083354414 cites W2046246382 @default.
- W2083354414 cites W2049169651 @default.
- W2083354414 cites W2052271603 @default.
- W2083354414 cites W2057081312 @default.
- W2083354414 cites W2058017150 @default.
- W2083354414 cites W2058101294 @default.
- W2083354414 cites W2062886670 @default.
- W2083354414 cites W2063565209 @default.
- W2083354414 cites W2067328535 @default.
- W2083354414 cites W2076261290 @default.
- W2083354414 cites W2079173335 @default.
- W2083354414 cites W2079179890 @default.
- W2083354414 cites W2080528351 @default.
- W2083354414 cites W2082679889 @default.
- W2083354414 cites W2085340024 @default.
- W2083354414 cites W2086441889 @default.
- W2083354414 cites W2087300555 @default.
- W2083354414 cites W2091969321 @default.
- W2083354414 cites W2097247190 @default.
- W2083354414 cites W2097493124 @default.
- W2083354414 cites W2100837269 @default.
- W2083354414 cites W2110958200 @default.
- W2083354414 cites W2112084742 @default.
- W2083354414 cites W2113964973 @default.
- W2083354414 cites W2127849149 @default.
- W2083354414 cites W2128266279 @default.
- W2083354414 cites W2131600643 @default.
- W2083354414 cites W2135975877 @default.
- W2083354414 cites W2138049414 @default.
- W2083354414 cites W2141084110 @default.
- W2083354414 cites W2142529984 @default.
- W2083354414 cites W2142786180 @default.
- W2083354414 cites W2143694829 @default.
- W2083354414 cites W2143869612 @default.
- W2083354414 cites W2144362290 @default.
- W2083354414 cites W2144483796 @default.
- W2083354414 cites W2144994678 @default.
- W2083354414 cites W2144998676 @default.
- W2083354414 cites W2147059525 @default.
- W2083354414 cites W2147402563 @default.
- W2083354414 cites W2148509534 @default.
- W2083354414 cites W2148641266 @default.
- W2083354414 cites W2158266834 @default.
- W2083354414 cites W2158714788 @default.
- W2083354414 cites W2170195050 @default.
- W2083354414 cites W2172000351 @default.
- W2083354414 cites W227623710 @default.
- W2083354414 cites W232616456 @default.
- W2083354414 cites W2517145217 @default.
- W2083354414 cites W265414167 @default.
- W2083354414 cites W4210400672 @default.
- W2083354414 cites W56031490 @default.
- W2083354414 cites W2066467301 @default.
- W2083354414 cites W4236268324 @default.
- W2083354414 doi "https://doi.org/10.1016/j.jmb.2006.02.056" @default.
- W2083354414 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16580018" @default.
- W2083354414 hasPublicationYear "2006" @default.