1ekm
From Proteopedia
(New page: 200px<br /><applet load="1ekm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ekm, resolution 2.50Å" /> '''CRYSTAL STRUCTURE AT...) |
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| - | [[Image:1ekm.gif|left|200px]]<br /><applet load="1ekm" size=" | + | [[Image:1ekm.gif|left|200px]]<br /><applet load="1ekm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ekm, resolution 2.50Å" /> | caption="1ekm, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI'''<br /> | '''CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Copper amine oxidases (CAOs) catalyze the two-electron oxidation of | + | Copper amine oxidases (CAOs) catalyze the two-electron oxidation of primary amines to aldehydes, utilizing molecular oxygen as a terminal electron acceptor. To accomplish this transformation, CAOs utilize two cofactors: a mononuclear copper, and a unique redox cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ or TOPA quinone). TPQ is derived via posttranslational modification of a specific tyrosine residue within the protein itself. In this study, the structure of an amine oxidase from Hansenula polymorpha has been solved to 2.5 A resolution, in which the precursor tyrosine is unprocessed to TPQ, and the copper site is occupied by zinc. Significantly, the precursor tyrosine directly ligands the metal, thus providing the closest analogue to date of an intermediate in TPQ production. Besides this result, the rearrangement of other active site residues (relative to the mature enzyme) proposed to be involved in the binding of molecular oxygen may shed light on how CAOs efficiently use their active site to carry out both cofactor formation and catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1EKM 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 ZN 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:// | + | 1EKM 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=ZN:'>ZN</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=1EKM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, Z.]] | [[Category: Chen, Z.]] | ||
| - | [[Category: Klinman, J | + | [[Category: Klinman, J P.]] |
[[Category: Li, R.]] | [[Category: Li, R.]] | ||
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
[[Category: Schwartz, B.]] | [[Category: Schwartz, B.]] | ||
| - | [[Category: Williams, N | + | [[Category: Williams, N K.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: amine oxidase]] | [[Category: amine oxidase]] | ||
[[Category: quinoprotein]] | [[Category: quinoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:48 2008'' |
Revision as of 10:28, 21 February 2008
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CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI
Overview
Copper amine oxidases (CAOs) catalyze the two-electron oxidation of primary amines to aldehydes, utilizing molecular oxygen as a terminal electron acceptor. To accomplish this transformation, CAOs utilize two cofactors: a mononuclear copper, and a unique redox cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ or TOPA quinone). TPQ is derived via posttranslational modification of a specific tyrosine residue within the protein itself. In this study, the structure of an amine oxidase from Hansenula polymorpha has been solved to 2.5 A resolution, in which the precursor tyrosine is unprocessed to TPQ, and the copper site is occupied by zinc. Significantly, the precursor tyrosine directly ligands the metal, thus providing the closest analogue to date of an intermediate in TPQ production. Besides this result, the rearrangement of other active site residues (relative to the mature enzyme) proposed to be involved in the binding of molecular oxygen may shed light on how CAOs efficiently use their active site to carry out both cofactor formation and catalysis.
About this Structure
1EKM 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
Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli., Chen Z, Schwartz B, Williams NK, Li R, Klinman JP, Mathews FS, Biochemistry. 2000 Aug 15;39(32):9709-17. PMID:10933787
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