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| - | [[Image:1avl.gif|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE== |
| - | |PDB= 1avl |SIZE=350|CAPTION= <scene name='initialview01'>1avl</scene>, resolution 2.8Å
| + | <StructureSection load='1avl' size='340' side='right'caption='[[1avl]], [[Resolution|resolution]] 2.80Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene> | + | <table><tr><td colspan='2'>[[1avl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVL FirstGlance]. <br> |
| - | |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>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1avl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avl OCA], [https://pdbe.org/1avl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avl RCSB], [https://www.ebi.ac.uk/pdbsum/1avl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avl ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1avl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avl OCA], [http://www.ebi.ac.uk/pdbsum/1avl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1avl RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1avl_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </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=1avl ConSurf]. |
| | + | <div style="clear:both"></div> |
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| - | '''CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE'''
| + | ==See Also== |
| - | | + | *[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | The crystal structures of the copper enzyme phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms of the enzyme: the holoenzyme in its active form (at 2.2 A resolution), the holoenzyme in an inactive form (at 2.8 A resolution), and the apoenzyme (at 2.2 A resolution). The holoenzyme has a topaquinone (TPQ) cofactor formed from the apoenzyme by the post-translational modification of a tyrosine residue in the presence of Cu2+. Significant differences between the three forms of AGAO are limited to the active site. The polypeptide fold is closely similar to those of the amine oxidases from Escherichia coli [Parsons, M. R., et al. (1995) Structure 3, 1171-1184] and pea seedlings [Kumar, V., et al. (1996) Structure 4, 943-955]. In the active form of holo-AGAO, the active-site Cu atom is coordinated by three His residues and two water molecules in an approximately square-pyramidal arrangement. In the inactive form, the Cu atom is coordinated by the same three His residues and by the phenolic oxygen of the TPQ, the geometry being quasi-trigonal-pyramidal. There is evidence of disorder in the crystals of both forms of holo-AGAO. As a result, only the position of the aromatic group of the TPQ cofactor, but not its orientation about the Cbeta-Cgamma bond, is determined unequivocally. In apo-AGAO, electron density consistent with an unmodified Tyr occurs at a position close to that of the TPQ in the inactive holo-AGAO. This observation has implications for the biogenesis of TPQ. Two features which have not been described previously in amine oxidase structures are a channel from the molecular surface to the active site and a solvent-filled cavity at the major interface between the two subunits of the dimer.
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| - | | + | |
| - | ==About this Structure==
| + | |
| - | 1AVL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVL OCA].
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| - | | + | |
| - | ==Reference==
| + | |
| - | Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone., Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H, Biochemistry. 1997 Dec 23;36(51):16116-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9405045 9405045]
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| - | [[Category: Amine oxidase (copper-containing)]]
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| | [[Category: Arthrobacter globiformis]] | | [[Category: Arthrobacter globiformis]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Freeman, H C.]] | + | [[Category: Freeman HC]] |
| - | [[Category: Guss, J M.]] | + | [[Category: Guss JM]] |
| - | [[Category: Wilce, M C.J.]] | + | [[Category: Wilce MCJ]] |
| - | [[Category: amine oxidase]]
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| - | [[Category: arthrobacter globiformi]]
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| - | [[Category: copper containing]]
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| - | [[Category: oxidoreductase]]
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:20 2008''
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