Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family
The crystal structure of the thaumatin-like xylanase inhibitor (TLXI) from Triticum aestivum, a non-competitive inhibitor of glycoside hydrolase family 11 xylanases, has been determined at 2.9 Å resolution. It is similar to that of thaumatin except that TLXI lacks domain II of thaumatin, making it t...
Gespeichert in:
| Veröffentlicht in: | Proteins-structure function and bioinformatics 2010-08, Vol.78 (10), p.2391-2394 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2394 |
|---|---|
| container_issue | 10 |
| container_start_page | 2391 |
| container_title | Proteins-structure function and bioinformatics |
| container_volume | 78 |
| creator | Vandermarliere, Elien Lammens, Willem Schoepe, Jan-Wolfgang Rombouts, Sigrid Fierens, Ellen Gebruers, Kurt Volckaert, Guido Rabijns, Anja Delcour, Jan Strelkov, Sergei Courtin, Christophe |
| description | The crystal structure of the thaumatin-like xylanase inhibitor (TLXI) from Triticum aestivum, a non-competitive inhibitor of glycoside hydrolase family 11 xylanases, has been determined at 2.9 Å resolution. It is similar to that of thaumatin except that TLXI lacks domain II of thaumatin, making it the first obtained crystallographic structure in the small thaumatin-like proteins (TLPs) subfamily within the larger family of TLPs. Unlike most other TLPs, TLXI does not contain the acidic surface cleft which is responsible for antifungal activity and binding of carbohydrates. Comparison with other TLPs suggests the loop containing histidine 22 as being important for xylanase inhibition. |
| format | Article |
| fullrecord | <record><control><sourceid>kuleuven</sourceid><recordid>TN_cdi_kuleuven_dspace_123456789_272548</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>123456789_272548</sourcerecordid><originalsourceid>FETCH-kuleuven_dspace_123456789_2725483</originalsourceid><addsrcrecordid>eNqVi7tOw0AQAK8AKYHwD9tRBEuOL7YvdRQEEmWKdNbGrJVN7mHd7UXx30MBPVQzxcydmpfGtIWuTT1TDymdy7JsNrqZq7iNUxK0kCTmXnIkCAPIicAH3wc3krDwleA2WfSYCNif-MgSIuw_Du8v4MgdKf5eyaG134bZobAvLF8IxhiE2MOAju20UPcD2kRPP3xUz6-7_fatuGRL-Uq--0wj9tStKr2um9Zsuqqt6rXR_ymXfys7uYn-ArWcWlk</addsrcrecordid><sourcetype>Institutional Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family</title><source>Lirias (KU Leuven Association)</source><source>Wiley Online Library All Journals</source><creator>Vandermarliere, Elien ; Lammens, Willem ; Schoepe, Jan-Wolfgang ; Rombouts, Sigrid ; Fierens, Ellen ; Gebruers, Kurt ; Volckaert, Guido ; Rabijns, Anja ; Delcour, Jan ; Strelkov, Sergei ; Courtin, Christophe</creator><creatorcontrib>Vandermarliere, Elien ; Lammens, Willem ; Schoepe, Jan-Wolfgang ; Rombouts, Sigrid ; Fierens, Ellen ; Gebruers, Kurt ; Volckaert, Guido ; Rabijns, Anja ; Delcour, Jan ; Strelkov, Sergei ; Courtin, Christophe</creatorcontrib><description>The crystal structure of the thaumatin-like xylanase inhibitor (TLXI) from Triticum aestivum, a non-competitive inhibitor of glycoside hydrolase family 11 xylanases, has been determined at 2.9 Å resolution. It is similar to that of thaumatin except that TLXI lacks domain II of thaumatin, making it the first obtained crystallographic structure in the small thaumatin-like proteins (TLPs) subfamily within the larger family of TLPs. Unlike most other TLPs, TLXI does not contain the acidic surface cleft which is responsible for antifungal activity and binding of carbohydrates. Comparison with other TLPs suggests the loop containing histidine 22 as being important for xylanase inhibition.</description><identifier>ISSN: 0887-3585</identifier><language>eng</language><publisher>Wiley-liss</publisher><ispartof>Proteins-structure function and bioinformatics, 2010-08, Vol.78 (10), p.2391-2394</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,316,782,786,27867</link.rule.ids></links><search><creatorcontrib>Vandermarliere, Elien</creatorcontrib><creatorcontrib>Lammens, Willem</creatorcontrib><creatorcontrib>Schoepe, Jan-Wolfgang</creatorcontrib><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Fierens, Ellen</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><creatorcontrib>Rabijns, Anja</creatorcontrib><creatorcontrib>Delcour, Jan</creatorcontrib><creatorcontrib>Strelkov, Sergei</creatorcontrib><creatorcontrib>Courtin, Christophe</creatorcontrib><title>Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family</title><title>Proteins-structure function and bioinformatics</title><description>The crystal structure of the thaumatin-like xylanase inhibitor (TLXI) from Triticum aestivum, a non-competitive inhibitor of glycoside hydrolase family 11 xylanases, has been determined at 2.9 Å resolution. It is similar to that of thaumatin except that TLXI lacks domain II of thaumatin, making it the first obtained crystallographic structure in the small thaumatin-like proteins (TLPs) subfamily within the larger family of TLPs. Unlike most other TLPs, TLXI does not contain the acidic surface cleft which is responsible for antifungal activity and binding of carbohydrates. Comparison with other TLPs suggests the loop containing histidine 22 as being important for xylanase inhibition.</description><issn>0887-3585</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>FZOIL</sourceid><recordid>eNqVi7tOw0AQAK8AKYHwD9tRBEuOL7YvdRQEEmWKdNbGrJVN7mHd7UXx30MBPVQzxcydmpfGtIWuTT1TDymdy7JsNrqZq7iNUxK0kCTmXnIkCAPIicAH3wc3krDwleA2WfSYCNif-MgSIuw_Du8v4MgdKf5eyaG134bZobAvLF8IxhiE2MOAju20UPcD2kRPP3xUz6-7_fatuGRL-Uq--0wj9tStKr2um9Zsuqqt6rXR_ymXfys7uYn-ArWcWlk</recordid><startdate>201008</startdate><enddate>201008</enddate><creator>Vandermarliere, Elien</creator><creator>Lammens, Willem</creator><creator>Schoepe, Jan-Wolfgang</creator><creator>Rombouts, Sigrid</creator><creator>Fierens, Ellen</creator><creator>Gebruers, Kurt</creator><creator>Volckaert, Guido</creator><creator>Rabijns, Anja</creator><creator>Delcour, Jan</creator><creator>Strelkov, Sergei</creator><creator>Courtin, Christophe</creator><general>Wiley-liss</general><scope>FZOIL</scope></search><sort><creationdate>201008</creationdate><title>Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family</title><author>Vandermarliere, Elien ; Lammens, Willem ; Schoepe, Jan-Wolfgang ; Rombouts, Sigrid ; Fierens, Ellen ; Gebruers, Kurt ; Volckaert, Guido ; Rabijns, Anja ; Delcour, Jan ; Strelkov, Sergei ; Courtin, Christophe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-kuleuven_dspace_123456789_2725483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vandermarliere, Elien</creatorcontrib><creatorcontrib>Lammens, Willem</creatorcontrib><creatorcontrib>Schoepe, Jan-Wolfgang</creatorcontrib><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Fierens, Ellen</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><creatorcontrib>Rabijns, Anja</creatorcontrib><creatorcontrib>Delcour, Jan</creatorcontrib><creatorcontrib>Strelkov, Sergei</creatorcontrib><creatorcontrib>Courtin, Christophe</creatorcontrib><collection>Lirias (KU Leuven Association)</collection><jtitle>Proteins-structure function and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vandermarliere, Elien</au><au>Lammens, Willem</au><au>Schoepe, Jan-Wolfgang</au><au>Rombouts, Sigrid</au><au>Fierens, Ellen</au><au>Gebruers, Kurt</au><au>Volckaert, Guido</au><au>Rabijns, Anja</au><au>Delcour, Jan</au><au>Strelkov, Sergei</au><au>Courtin, Christophe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family</atitle><jtitle>Proteins-structure function and bioinformatics</jtitle><date>2010-08</date><risdate>2010</risdate><volume>78</volume><issue>10</issue><spage>2391</spage><epage>2394</epage><pages>2391-2394</pages><issn>0887-3585</issn><abstract>The crystal structure of the thaumatin-like xylanase inhibitor (TLXI) from Triticum aestivum, a non-competitive inhibitor of glycoside hydrolase family 11 xylanases, has been determined at 2.9 Å resolution. It is similar to that of thaumatin except that TLXI lacks domain II of thaumatin, making it the first obtained crystallographic structure in the small thaumatin-like proteins (TLPs) subfamily within the larger family of TLPs. Unlike most other TLPs, TLXI does not contain the acidic surface cleft which is responsible for antifungal activity and binding of carbohydrates. Comparison with other TLPs suggests the loop containing histidine 22 as being important for xylanase inhibition.</abstract><pub>Wiley-liss</pub><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0887-3585 |
| ispartof | Proteins-structure function and bioinformatics, 2010-08, Vol.78 (10), p.2391-2394 |
| issn | 0887-3585 |
| language | eng |
| recordid | cdi_kuleuven_dspace_123456789_272548 |
| source | Lirias (KU Leuven Association); Wiley Online Library All Journals |
| title | Crystal structure of the noncompetitive xylanase inhibitor TLXI, member of the small thaumatin-like protein family |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T02%3A15%3A24IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-kuleuven&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystal%20structure%20of%20the%20noncompetitive%20xylanase%20inhibitor%20TLXI,%20member%20of%20the%20small%20thaumatin-like%20protein%20family&rft.jtitle=Proteins-structure%20function%20and%20bioinformatics&rft.au=Vandermarliere,%20Elien&rft.date=2010-08&rft.volume=78&rft.issue=10&rft.spage=2391&rft.epage=2394&rft.pages=2391-2394&rft.issn=0887-3585&rft_id=info:doi/&rft_dat=%3Ckuleuven%3E123456789_272548%3C/kuleuven%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true |