1ta3
From Proteopedia
(New page: 200px<br /><applet load="1ta3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ta3, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ta3.gif|left|200px]]<br /><applet load="1ta3" size=" | + | [[Image:1ta3.gif|left|200px]]<br /><applet load="1ta3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ta3, resolution 1.70Å" /> | caption="1ta3, resolution 1.70Å" /> | ||
'''Crystal Structure of xylanase (GH10) in complex with inhibitor (XIP)'''<br /> | '''Crystal Structure of xylanase (GH10) in complex with inhibitor (XIP)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The xylanase inhibitor protein I (XIP-I) from wheat Triticum aestivum is | + | The xylanase inhibitor protein I (XIP-I) from wheat Triticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 A resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold. Inhibition of the GH11 xylanase is mediated by the insertion of an XIP-I Pi-shaped loop (Lalpha(4)beta(5)) into the enzyme active site, whereas residues in the helix alpha7 of XIP-I, pointing into the four central active site subsites, are mainly responsible for the reversible inactivation of GH10 xylanases. The XIP-I strategy for inhibition of xylanases involves substrate-mimetic contacts and interactions occluding the active site. The structural determinants of XIP-I specificity demonstrate that the inhibitor is able to interact with GH10 and GH11 xylanases of both fungal and bacterial origin. The biological role of the xylanase inhibitors is discussed in light of the present structural data. |
==About this Structure== | ==About this Structure== | ||
| - | 1TA3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with NAG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1TA3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans] and [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1TA3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Durand, A.]] | [[Category: Durand, A.]] | ||
[[Category: Furniss, C.]] | [[Category: Furniss, C.]] | ||
| - | [[Category: Gilbert, H | + | [[Category: Gilbert, H J.]] |
[[Category: Juge, N.]] | [[Category: Juge, N.]] | ||
[[Category: Leone, P.]] | [[Category: Leone, P.]] | ||
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[[Category: beta alpha barrel (xylanase)]] | [[Category: beta alpha barrel (xylanase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:31 2008'' |
Revision as of 13:11, 21 February 2008
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Crystal Structure of xylanase (GH10) in complex with inhibitor (XIP)
Overview
The xylanase inhibitor protein I (XIP-I) from wheat Triticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 A resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold. Inhibition of the GH11 xylanase is mediated by the insertion of an XIP-I Pi-shaped loop (Lalpha(4)beta(5)) into the enzyme active site, whereas residues in the helix alpha7 of XIP-I, pointing into the four central active site subsites, are mainly responsible for the reversible inactivation of GH10 xylanases. The XIP-I strategy for inhibition of xylanases involves substrate-mimetic contacts and interactions occluding the active site. The structural determinants of XIP-I specificity demonstrate that the inhibitor is able to interact with GH10 and GH11 xylanases of both fungal and bacterial origin. The biological role of the xylanase inhibitors is discussed in light of the present structural data.
About this Structure
1TA3 is a Protein complex structure of sequences from Emericella nidulans and Triticum aestivum with and as ligands. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases., Payan F, Leone P, Porciero S, Furniss C, Tahir T, Williamson G, Durand A, Manzanares P, Gilbert HJ, Juge N, Roussel A, J Biol Chem. 2004 Aug 20;279(34):36029-37. Epub 2004 Jun 4. PMID:15181003
Page seeded by OCA on Thu Feb 21 15:11:31 2008
Categories: Emericella nidulans | Endo-1,4-beta-xylanase | Protein complex | Triticum aestivum | Durand, A. | Furniss, C. | Gilbert, H J. | Juge, N. | Leone, P. | Manzanares, P. | Payan, F. | Porciero, S. | Roussel, A. | Tahir, T. | Williamson, G. | EDO | NAG | Beta alpha barrel (xip-i) | Beta alpha barrel (xylanase)
