1wno

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(New page: 200px<br /><applet load="1wno" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wno, resolution 2.10&Aring;" /> '''Crystal structure of...)
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caption="1wno, resolution 2.10&Aring;" />
'''Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407'''<br />
'''Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407'''<br />
==Overview==
==Overview==
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Chitinase hydrolyzes chitin, a linear polymer of beta-1,4-linked, N-acetylglucosamine (NAG), and plays a variety of roles in the biological, world. In addition to endo- and exo-hydrolytic activities, transglycosyl, activity has also been observed in the extracellular chitinase (afCHI), from the airborne saprophytic fungi Aspergillus fumigatus YJ-407. Crystals, of this native chitinase have been grown at 291 K using PEG 3350 as a, precipitant. The diffraction data from the crystal extend to 1.7 A, resolution at BSRF, China. The crystal belongs to space group, P2(1)2(1)2(1), with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 A., The presence of two molecules per asymmetric unit gives a crystal volume, per protein mass (V(M)) of 3.6 A(3) Da(-1) and a solvent content of 65% by, volume. A full set of X-ray diffraction data was collected to 2.1 A, resolution.
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Chitinase hydrolyzes chitin, a linear polymer of beta-1,4-linked N-acetylglucosamine (NAG), and plays a variety of roles in the biological world. In addition to endo- and exo-hydrolytic activities, transglycosyl activity has also been observed in the extracellular chitinase (afCHI) from the airborne saprophytic fungi Aspergillus fumigatus YJ-407. Crystals of this native chitinase have been grown at 291 K using PEG 3350 as a precipitant. The diffraction data from the crystal extend to 1.7 A resolution at BSRF, China. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 A. The presence of two molecules per asymmetric unit gives a crystal volume per protein mass (V(M)) of 3.6 A(3) Da(-1) and a solvent content of 65% by volume. A full set of X-ray diffraction data was collected to 2.1 A resolution.
==About this Structure==
==About this Structure==
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1WNO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus] with NDG, NAG, SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WNO OCA].
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1WNO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNO OCA].
==Reference==
==Reference==
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[[Category: eight-stranded beta/alpha-barrel]]
[[Category: eight-stranded beta/alpha-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:22:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:18 2008''

Revision as of 13:46, 21 February 2008

Image:1wno.gif

1wno, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407

Overview

Chitinase hydrolyzes chitin, a linear polymer of beta-1,4-linked N-acetylglucosamine (NAG), and plays a variety of roles in the biological world. In addition to endo- and exo-hydrolytic activities, transglycosyl activity has also been observed in the extracellular chitinase (afCHI) from the airborne saprophytic fungi Aspergillus fumigatus YJ-407. Crystals of this native chitinase have been grown at 291 K using PEG 3350 as a precipitant. The diffraction data from the crystal extend to 1.7 A resolution at BSRF, China. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 95.7, b = 100.5, c = 134.3 A. The presence of two molecules per asymmetric unit gives a crystal volume per protein mass (V(M)) of 3.6 A(3) Da(-1) and a solvent content of 65% by volume. A full set of X-ray diffraction data was collected to 2.1 A resolution.

About this Structure

1WNO is a Single protein structure of sequence from Aspergillus fumigatus with , , and as ligands. Active as Chitinase, with EC number 3.2.1.14 Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary crystallographic analysis of a native chitinase from the fungal pathogen Aspergillus fumigatus YJ-407., Hu H, Wang G, Yang H, Zhou J, Mo L, Yang K, Jin C, Jin C, Rao Z, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):939-40. Epub 2004, Apr 21. PMID:15103145

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