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1te1

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Revision as of 11:49, 24 December 2020

Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)

Structural highlights

1te1 is a 2 chain structure with sequence from Cbs 272.86 and Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	xynC (CBS 272.86)
Activity:	Endo-1,4-beta-xylanase, with EC number 3.2.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[XIP1_WHEAT] Fungal xylanase inhibitor. Possesses competitive inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). Possesses also inhibitory activity towards barley alpha-amylases. Binding to xylanases or amylases is necessary for inhibition activity. May function in plant defense against secreted fungal pathogen xylanases. Is similar to class III chitinases, but does not exhibit chitinase activity.^[1] ^[2] ^[3] ^[4] [XYNC_PENFN] Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The xylanase inhibitor protein I (XIP-I) from wheat Triticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 A resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold. Inhibition of the GH11 xylanase is mediated by the insertion of an XIP-I Pi-shaped loop (Lalpha(4)beta(5)) into the enzyme active site, whereas residues in the helix alpha7 of XIP-I, pointing into the four central active site subsites, are mainly responsible for the reversible inactivation of GH10 xylanases. The XIP-I strategy for inhibition of xylanases involves substrate-mimetic contacts and interactions occluding the active site. The structural determinants of XIP-I specificity demonstrate that the inhibitor is able to interact with GH10 and GH11 xylanases of both fungal and bacterial origin. The biological role of the xylanase inhibitors is discussed in light of the present structural data.

The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases.,Payan F, Leone P, Porciero S, Furniss C, Tahir T, Williamson G, Durand A, Manzanares P, Gilbert HJ, Juge N, Roussel A J Biol Chem. 2004 Aug 20;279(34):36029-37. Epub 2004 Jun 4. PMID:15181003^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Elliott GO, Hughes RK, Juge N, Kroon PA, Williamson G. Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-xylanase inhibitor. FEBS Lett. 2002 May 22;519(1-3):66-70. PMID:12023019
↑ McLauchlan WR, Garcia-Conesa MT, Williamson G, Roza M, Ravestein P, Maat J. A novel class of protein from wheat which inhibits xylanases. Biochem J. 1999 Mar 1;338 ( Pt 2):441-6. PMID:10024521
↑ Flatman R, McLauchlan WR, Juge N, Furniss C, Berrin JG, Hughes RK, Manzanares P, Ladbury JE, O'Brien R, Williamson G. Interactions defining the specificity between fungal xylanases and the xylanase-inhibiting protein XIP-I from wheat. Biochem J. 2002 Aug 1;365(Pt 3):773-81. PMID:11955286 doi:http://dx.doi.org/10.1042/BJ20020168
↑ Sancho AI, Faulds CB, Svensson B, Bartolome B, Williamson G, Juge N. Cross-inhibitory activity of cereal protein inhibitors against alpha-amylases and xylanases. Biochim Biophys Acta. 2003 Aug 21;1650(1-2):136-44. PMID:12922177
↑ Payan F, Leone P, Porciero S, Furniss C, Tahir T, Williamson G, Durand A, Manzanares P, Gilbert HJ, Juge N, Roussel A. The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases. J Biol Chem. 2004 Aug 20;279(34):36029-37. Epub 2004 Jun 4. PMID:15181003 doi:10.1074/jbc.M404225200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1te1"

@@ Line 1: / Line 1: @@
 ==Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)==
-<StructureSection load='1te1' size='340' side='right' caption='[[1te1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='1te1' size='340' side='right'caption='[[1te1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1te1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_272.86 Cbs 272.86] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TE1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1te1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_272.86 Cbs 272.86] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TE1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xynC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28572 CBS 272.86])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=1te1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te1 OCA], [http://pdbe.org/1te1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1te1 RCSB], [http://www.ebi.ac.uk/pdbsum/1te1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1te1 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1te1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te1 OCA], [http://pdbe.org/1te1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1te1 RCSB], [http://www.ebi.ac.uk/pdbsum/1te1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1te1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 36: / Line 36: @@
 [[Category: Cbs 272 86]]
 [[Category: Endo-1,4-beta-xylanase]]
+[[Category: Large Structures]]
 [[Category: Triticum aestivum]]
 [[Category: Durand, A]]

1te1

From Proteopedia

Revision as of 11:49, 24 December 2020

Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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