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1avk

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[[Image:1avk.gif|left|200px]]
 
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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==
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The line below this paragraph, containing "STRUCTURE_1avk", creates the "Structure Box" on the page.
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<StructureSection load='1avk' size='340' side='right'caption='[[1avk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1avk]] 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=1AVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AVK FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#8491;</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=1avk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1avk OCA], [https://pdbe.org/1avk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1avk RCSB], [https://www.ebi.ac.uk/pdbsum/1avk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1avk ProSAT]</span></td></tr>
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{{STRUCTURE_1avk| PDB=1avk | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO]
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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/av/1avk_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=1avk ConSurf].
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<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'''
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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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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==
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1AVK 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=1AVK OCA].
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==Reference==
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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 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: Arthrobacter globiformis]]
[[Category: Arthrobacter globiformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Freeman, H C.]]
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[[Category: Freeman HC]]
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[[Category: Guss, J M.]]
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[[Category: Guss JM]]
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[[Category: Tanizawa, K.]]
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[[Category: Tanizawa K]]
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[[Category: Wilce, M C.J.]]
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[[Category: Wilce MCJ]]
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[[Category: Yamaguchi, H.]]
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[[Category: Yamaguchi H]]
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[[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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[[Category: Quinone]]
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[[Category: Tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:44:38 2008''
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Current revision

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 ID 1avk

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