This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1t6e
From Proteopedia
(New page: 200px<br /><applet load="1t6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6e, resolution 1.70Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1t6e.jpg|left|200px]]<br /><applet load="1t6e" size=" | + | [[Image:1t6e.jpg|left|200px]]<br /><applet load="1t6e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t6e, resolution 1.70Å" /> | caption="1t6e, resolution 1.70Å" /> | ||
'''Crystal Structure of the Triticum aestivum xylanase inhibitor I'''<br /> | '''Crystal Structure of the Triticum aestivum xylanase inhibitor I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Plants developed a diverse battery of defense mechanisms in response to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1T6E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T6E OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
[[Category: Brijs, K.]] | [[Category: Brijs, K.]] | ||
| - | [[Category: Courtin, C | + | [[Category: Courtin, C M.]] |
| - | [[Category: Delcour, J | + | [[Category: Delcour, J A.]] |
[[Category: Gebruers, K.]] | [[Category: Gebruers, K.]] | ||
[[Category: Rabijns, A.]] | [[Category: Rabijns, A.]] | ||
| - | [[Category: Ranter, C | + | [[Category: Ranter, C J.De.]] |
[[Category: Sansen, S.]] | [[Category: Sansen, S.]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: two beta-barrel domain structure]] | [[Category: two beta-barrel domain structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:19 2008'' |
Revision as of 13:10, 21 February 2008
|
Crystal Structure of the Triticum aestivum xylanase inhibitor I
Overview
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.
About this Structure
1T6E is a Single protein structure of sequence from Triticum aestivum with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:10:19 2008
