1ekm

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[[Image:1ekm.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI==
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|PDB= 1ekm |SIZE=350|CAPTION= <scene name='initialview01'>1ekm</scene>, resolution 2.50&Aring;
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<StructureSection load='1ekm' size='340' side='right'caption='[[1ekm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1ekm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EKM FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ekm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ekm OCA], [https://pdbe.org/1ekm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ekm RCSB], [https://www.ebi.ac.uk/pdbsum/1ekm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ekm ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1a2v|1A2V]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ekm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ekm OCA], [http://www.ebi.ac.uk/pdbsum/1ekm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ekm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMO_PICAN AMO_PICAN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1ekm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ekm ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI'''
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==See Also==
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Ogataea angusta]]
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==About this Structure==
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[[Category: Chen Z]]
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1EKM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_angusta Pichia angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKM OCA].
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[[Category: Klinman JP]]
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[[Category: Li R]]
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==Reference==
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[[Category: Mathews FS]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10933787 10933787]
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[[Category: Schwartz B]]
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[[Category: Amine oxidase (copper-containing)]]
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[[Category: Williams NK]]
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[[Category: Pichia angusta]]
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[[Category: Single protein]]
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[[Category: Chen, Z.]]
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[[Category: Klinman, J P.]]
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[[Category: Li, R.]]
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[[Category: Mathews, F S.]]
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[[Category: Schwartz, B.]]
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[[Category: Williams, N K.]]
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[[Category: amine oxidase]]
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[[Category: quinoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:04:28 2008''
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Current revision

CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI

PDB ID 1ekm

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