1t6g
From Proteopedia
(New page: 200px<br /><applet load="1t6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t6g, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1t6g.jpg|left|200px]]<br /><applet load="1t6g" size=" | + | [[Image:1t6g.jpg|left|200px]]<br /><applet load="1t6g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t6g, resolution 1.80Å" /> | caption="1t6g, resolution 1.80Å" /> | ||
'''Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-I'''<br /> | '''Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-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== | ||
| - | 1T6G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] and [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:// | + | 1T6G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] and [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=1T6G OCA]. |
==Reference== | ==Reference== | ||
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[[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]] | ||
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[[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 15:10:26 2008'' |
Revision as of 13:10, 21 February 2008
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Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-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
1T6G is a Protein complex structure of sequences from Aspergillus niger and 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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