3A71
High resolution structure of Penicillium chrysogenum alpha-L-arabinanase
Summary for 3A71
| Entry DOI | 10.2210/pdb3a71/pdb |
| Related | 3A72 |
| Descriptor | Exo-arabinanase, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | arabinase, glycosyl hydrolase, hydrolase |
| Biological source | Penicillium chrysogenum (Penicillium notatum) |
| Total number of polymer chains | 1 |
| Total formula weight | 39773.19 |
| Authors | Sogabe, Y. (deposition date: 2009-09-11, release date: 2010-09-15, Last modification date: 2024-03-13) |
| Primary citation | Sogabe, Y.,Kitatani, T.,Yamaguchi, A.,Kinoshita, T.,Adachi, H.,Takano, K.,Inoue, T.,Mori, Y.,Matsumura, H.,Sakamoto, T.,Tada, T. High-resolution structure of exo-arabinanase from Penicillium chrysogenum Acta Crystallogr.,Sect.D, 67:415-422, 2011 Cited by PubMed Abstract: Arabinanase Abnx from Penicillium chrysogenum 31B, which belongs to the GH93 family, releases arabinobiose from the nonreducing terminus of α-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 Å to an R(work) of 10.7% (R(free) = 12.8%) and 1.04 Å to an R(work) of 10.4% (R(free) = 12.5%). Abnx has a six-bladed β-propeller fold with a typical ring-closure mode called `Velcro', in which the last four-stranded β-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. PubMed: 21543843DOI: 10.1107/S0907444911006299 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.14 Å) |
Structure validation
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