1d6u

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[[Image:1d6u.gif|left|200px]]<br /><applet load="1d6u" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d6u, resolution 2.4&Aring;" />
 
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'''CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE==
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X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.
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<StructureSection load='1d6u' size='340' side='right'caption='[[1d6u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d6u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D6U FirstGlance]. <br>
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene>, <scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene>, <scene name='pdbligand=TYQ:3-AMINO-6-HYDROXY-TYROSINE'>TYQ</scene></td></tr>
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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=1d6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6u OCA], [https://pdbe.org/1d6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d6u RCSB], [https://www.ebi.ac.uk/pdbsum/1d6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d6u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMO_ECOLI AMO_ECOLI] The enzyme prefers aromatic over aliphatic amines.
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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/d6/1d6u_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=1d6u ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D6U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HY1:'>HY1</scene>, <scene name='pdbligand=PEA:'>PEA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1D6U OCA].
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10576737 10576737]
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[[Category: Amine oxidase (copper-containing)]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hajdu, J.]]
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[[Category: Hajdu J]]
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[[Category: Knowles, P F.]]
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[[Category: Knowles PF]]
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[[Category: McPherson, M J.]]
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[[Category: McPherson MJ]]
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[[Category: Phillips, S E.V.]]
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[[Category: Phillips SEV]]
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[[Category: Wilmot, C M.]]
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[[Category: Wilmot CM]]
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[[Category: CA]]
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[[Category: CU]]
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[[Category: GOL]]
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[[Category: HY1]]
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[[Category: PEA]]
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[[Category: reaction intermediate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:35 2008''
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Current revision

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE

PDB ID 1d6u

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