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1wno
From Proteopedia
(New page: 200px<br /><applet load="1wno" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wno, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1wno.gif|left|200px]]<br /><applet load="1wno" size=" | + | [[Image:1wno.gif|left|200px]]<br /><applet load="1wno" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wno, resolution 2.10Å" /> | caption="1wno, resolution 2.10Å" /> | ||
'''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== | ||
| - | Chitinase hydrolyzes chitin, a linear polymer of beta-1,4-linked | + | 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== | ||
| - | 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:// | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 15:46:18 2008
Categories: Aspergillus fumigatus | Chitinase | Single protein | Hu, H. | Jin, C. | Mo, L. | Rao, Z. | Wang, G. | Yang, H. | Yang, K. | Zhou, J. | MG | NAG | NDG | SO4 | Eight-stranded beta/alpha-barrel
