1t6e

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(New page: 200px<br /><applet load="1t6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6e, resolution 1.70&Aring;" /> '''Crystal Structure of...)
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caption="1t6e, resolution 1.70&Aring;" />
'''Crystal Structure of the Triticum aestivum xylanase inhibitor I'''<br />
'''Crystal Structure of the Triticum aestivum xylanase inhibitor I'''<br />
==Overview==
==Overview==
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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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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T6E OCA].
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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==
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[[Category: Triticum aestivum]]
[[Category: Triticum aestivum]]
[[Category: Brijs, K.]]
[[Category: Brijs, K.]]
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[[Category: Courtin, C.M.]]
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[[Category: Courtin, C M.]]
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[[Category: Delcour, J.A.]]
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[[Category: Delcour, J A.]]
[[Category: Gebruers, K.]]
[[Category: Gebruers, K.]]
[[Category: Rabijns, A.]]
[[Category: Rabijns, A.]]
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[[Category: Ranter, C.J.De.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:44:46 2007''
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''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


1t6e, resolution 1.70Å

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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

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