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New page: left|200px<br /><applet load="1avl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avl, resolution 2.8Å" /> '''CRYSTAL STRUCTURES OF...
 
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[[Image:1avl.gif|left|200px]]<br /><applet load="1avl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1avl, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE'''<br />


==Overview==
==CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE==
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.
<StructureSection load='1avl' size='340' side='right'caption='[[1avl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<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>
<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>
</table>
== 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>


==About this Structure==
==See Also==
1AVL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AVL OCA].
*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9405045 9405045]
[[Category: Amine oxidase (copper-containing)]]
[[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: CU]]
[[Category: amine oxidase]]
[[Category: arthrobacter globiformis]]
[[Category: copper containing]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:09:37 2007''

Latest revision as of 15:28, 13 March 2024

CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE

1avl, resolution 2.80Å

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