Structural highlights
3rwk is a 1 chain structure with sequence from Aspergillus ficuum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , , , , , , |
Activity: | Inulinase, with EC number 3.2.1.7 |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[INU2_ASPFI] Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60.[1]
Publication Abstract from PubMed
Endo-inulinase is a member of glycosidase hydrolase family 32 (GH32) degrading fructans of the inulin type with an endo-cleavage mode and is an important class of industrial enzyme. In the present study, we report the first crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum at 1.5 A. It was solved by molecular replacement with the structure of exo-inulinase as search model. The 3D structure presents a bimodular arrangement common to other GH32 enzymes: a N-terminal 5-fold beta-propeller catalytic domain with four beta-sheets and a C-terminal beta-sandwich domain organized in two beta-sheets with five beta-strands. The structural analysis and comparison with other GH32 enzymes reveal the presence of an extra pocket in the INU2 catalytic site, formed by two loops and the conserved motif W-M(I)-N-D(E)-P-N-G. This cavity would explain the endo-activity of the enzyme, the critical role of Trp40 and particularly the cleavage at the third unit of the inulin(-like) substrates. Crystal structure at 2.1 A of INU2 complexed with fructosyl molecules, experimental digestion data and molecular modelling studies support these hypotheses.
First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity.,Pouyez J, Mayard A, Vandamme AM, Roussel G, Perpete EA, Wouters J, Housen I, Michaux C Biochimie. 2012 Jun 28. PMID:22750808[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vandamme AM, Michaux C, Mayard A, Housen I. Asparagine 42 of the conserved endo-inulinase INU2 motif WMNDPN from Aspergillus ficuum plays a role in activity specificity. FEBS Open Bio. 2013 Nov 1;3:467-72. doi: 10.1016/j.fob.2013.10.009. eCollection, 2013. PMID:24251113 doi:http://dx.doi.org/10.1016/j.fob.2013.10.009
- ↑ Pouyez J, Mayard A, Vandamme AM, Roussel G, Perpete EA, Wouters J, Housen I, Michaux C. First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity. Biochimie. 2012 Jun 28. PMID:22750808 doi:10.1016/j.biochi.2012.06.020