2dfc

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(New page: 200px<br /><applet load="2dfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dfc, resolution 1.19&Aring;" /> '''Xylanase II from Tri...)
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[[Image:2dfc.gif|left|200px]]<br /><applet load="2dfc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2dfc, resolution 1.19&Aring;" />
caption="2dfc, resolution 1.19&Aring;" />
'''Xylanase II from Tricoderma reesei at 293K'''<br />
'''Xylanase II from Tricoderma reesei at 293K'''<br />
==Overview==
==Overview==
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An orthorhombic crystal of xylanase II from Trichoderma reesei was grown, in the presence of sodium iodide. Crystal structures at atomic resolution, were determined at 100 and 293 K. Protein molecules were aligned along a, crystallographic twofold screw axis, forming a helically extended, polymer-like chain mediated by an iodide ion. The iodide ion connected, main-chain peptide groups between two adjacent molecules by an, N-H...I-...H-N hydrogen-bond bridge, thus contributing to regulation of, the molecular arrangement and suppression of the rigid-body motion in the, crystal with high diffraction quality. The structure at 293 K showed, considerable thermal motion in the loop regions connecting the, beta-strands that form the active-site cleft. TLS model analysis of the, thermal motion and a comparison between this structure and that at 100 K, suggest that the fluctuation of these loop regions is attributable to the, hinge-like movement of the beta-strands.
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An orthorhombic crystal of xylanase II from Trichoderma reesei was grown in the presence of sodium iodide. Crystal structures at atomic resolution were determined at 100 and 293 K. Protein molecules were aligned along a crystallographic twofold screw axis, forming a helically extended polymer-like chain mediated by an iodide ion. The iodide ion connected main-chain peptide groups between two adjacent molecules by an N-H...I-...H-N hydrogen-bond bridge, thus contributing to regulation of the molecular arrangement and suppression of the rigid-body motion in the crystal with high diffraction quality. The structure at 293 K showed considerable thermal motion in the loop regions connecting the beta-strands that form the active-site cleft. TLS model analysis of the thermal motion and a comparison between this structure and that at 100 K suggest that the fluctuation of these loop regions is attributable to the hinge-like movement of the beta-strands.
==About this Structure==
==About this Structure==
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2DFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with IOD 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=2DFC OCA].
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2DFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=IOD:'>IOD</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=2DFC OCA].
==Reference==
==Reference==
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[[Category: bent beta sheet]]
[[Category: bent beta sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:34:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:58:13 2008''

Revision as of 14:58, 21 February 2008


2dfc, resolution 1.19Å

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Xylanase II from Tricoderma reesei at 293K

Overview

An orthorhombic crystal of xylanase II from Trichoderma reesei was grown in the presence of sodium iodide. Crystal structures at atomic resolution were determined at 100 and 293 K. Protein molecules were aligned along a crystallographic twofold screw axis, forming a helically extended polymer-like chain mediated by an iodide ion. The iodide ion connected main-chain peptide groups between two adjacent molecules by an N-H...I-...H-N hydrogen-bond bridge, thus contributing to regulation of the molecular arrangement and suppression of the rigid-body motion in the crystal with high diffraction quality. The structure at 293 K showed considerable thermal motion in the loop regions connecting the beta-strands that form the active-site cleft. TLS model analysis of the thermal motion and a comparison between this structure and that at 100 K suggest that the fluctuation of these loop regions is attributable to the hinge-like movement of the beta-strands.

About this Structure

2DFC is a Single protein structure of sequence from Hypocrea jecorina 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

Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement., Watanabe N, Akiba T, Kanai R, Harata K, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):784-92. Epub 2006, Jun 20. PMID:16790934

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