1a2v
From Proteopedia
(New page: 200px<br /><applet load="1a2v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a2v, resolution 2.40Å" /> '''COPPER AMINE OXIDASE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1a2v.gif|left|200px]]<br /><applet load="1a2v" size=" | + | [[Image:1a2v.gif|left|200px]]<br /><applet load="1a2v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a2v, resolution 2.40Å" /> | caption="1a2v, resolution 2.40Å" /> | ||
'''COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA'''<br /> | '''COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The copper-containing amine oxidase from the yeast Hansenula polymorpha | + | The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson & Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress. |
==About this Structure== | ==About this Structure== | ||
| - | 1A2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_angusta Pichia angusta] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http:// | + | 1A2V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_angusta Pichia angusta] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2V OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Li, R.]] | [[Category: Li, R.]] | ||
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: amine oxidase]] | [[Category: amine oxidase]] | ||
| Line 22: | Line 22: | ||
[[Category: tpq]] | [[Category: tpq]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:13 2008'' |
Revision as of 09:40, 21 February 2008
|
COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Overview
The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson & Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress.
About this Structure
1A2V is a Single protein structure of sequence from Pichia angusta with as ligand. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.
Reference
Crystallographic study of yeast copper amine oxidase., Li R, Chen L, Cai D, Klinman JP, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):364-70. PMID:15299901
Page seeded by OCA on Thu Feb 21 11:40:13 2008
