1ekm
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(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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Revision as of 11:57, 20 November 2007
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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 ZN 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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