3a72
High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobioseHigh resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedArabinanase Abnx from Penicillium chrysogenum 31B, which belongs to the GH93 family, releases arabinobiose from the nonreducing terminus of alpha-1,5-L-arabinan, which is distributed in the primary cell walls of higher plants. Crystal structures of Abnx and of its complex with arabinobiose were determined at the high resolutions of 1.14 A to an R(work) of 10.7% (R(free) = 12.8%) and 1.04 A to an R(work) of 10.4% (R(free) = 12.5%). Abnx has a six-bladed beta-propeller fold with a typical ring-closure mode called `Velcro', in which the last four-stranded beta-sheet is completed by the incorporation of a strand from the N-terminus. Catalytic residues which act as a nucleophile and an acid/base were proposed from the structures and confirmed by site-directed mutagenesis. The substrate-binding groove is enclosed at one end by two residues, Glu64 and Tyr66, which contribute to the recognition of the nonreducing chain end of the polysaccharide. A comparison with the related enzyme Arb93A which has a quite similar overall structure suggested that Abnx has different mechanisms to funnel substrates to the active site and/or to stabilize the transition state. High-resolution structure of exo-arabinanase from Penicillium chrysogenum.,Sogabe Y, Kitatani T, Yamaguchi A, Kinoshita T, Adachi H, Takano K, Inoue T, Mori Y, Matsumura H, Sakamoto T, Tada T Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):415-22. Epub 2011, Apr 13. PMID:21543843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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