1t6e

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1t6e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T6E FirstGlance]. <br>
<table><tr><td colspan='2'>[[1t6e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T6E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6e OCA], [https://pdbe.org/1t6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t6e RCSB], [https://www.ebi.ac.uk/pdbsum/1t6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6e ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t6e OCA], [https://pdbe.org/1t6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t6e RCSB], [https://www.ebi.ac.uk/pdbsum/1t6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t6e ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8H0K8_WHEAT Q8H0K8_WHEAT]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t6e ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t6e ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. The structure of Triticum aestivum xylanase inhibitor-I (TAXI-I), a first member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases, has been determined to 1.7-A resolution. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytical triad are absent. The structure of the TAXI-I.Aspergillus niger xylanase I complex, at a resolution of 1.8 A, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors.
 
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Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I.,Sansen S, De Ranter CJ, Gebruers K, Brijs K, Courtin CM, Delcour JA, Rabijns A J Biol Chem. 2004 Aug 20;279(34):36022-8. Epub 2004 May 27. PMID:15166216<ref>PMID:15166216</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1t6e" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endo-1,4-beta-xylanase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Triticum aestivum]]
[[Category: Triticum aestivum]]
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[[Category: Brijs, K]]
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[[Category: Brijs K]]
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[[Category: Courtin, C M]]
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[[Category: Courtin CM]]
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[[Category: Delcour, J A]]
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[[Category: De Ranter CJ]]
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[[Category: Gebruers, K]]
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[[Category: Delcour JA]]
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[[Category: Rabijns, A]]
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[[Category: Gebruers K]]
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[[Category: Ranter, C J.De]]
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[[Category: Rabijns A]]
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[[Category: Sansen, S]]
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[[Category: Sansen S]]
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[[Category: Hydrolase inhibitor]]
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[[Category: Two beta-barrel domain structure]]
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Revision as of 08:38, 1 May 2024

Crystal Structure of the Triticum aestivum xylanase inhibitor I

PDB ID 1t6e

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