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3rwk

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Revision as of 06:10, 5 August 2016

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

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.
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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3rwk"

@@ Line 1: / Line 1: @@
 ==First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.==
 <StructureSection load='3rwk' size='340' side='right' caption='[[3rwk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inulinase Inulinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.7 3.2.1.7] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rwk RCSB], [http://www.ebi.ac.uk/pdbsum/3rwk PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwk OCA], [http://pdbe.org/3rwk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rwk RCSB], [http://www.ebi.ac.uk/pdbsum/3rwk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rwk ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3rwk" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3rwk

From Proteopedia

Revision as of 06:10, 5 August 2016

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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