1iqx: Difference between revisions

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New page: left|200px<br /><applet load="1iqx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iqx, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1iqx.jpg|left|200px]]<br /><applet load="1iqx" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF COBALT-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF COBALT-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS==
The role of the active site Cu(2+) of phenylethylamine oxidase from, Arthrobacter globiformis (AGAO) has been studied by substitution with, other divalent cations, where we were able to remove &gt;99.5% of Cu(2+) from, the active site. The enzymes reconstituted with Co(2+) and Ni(2+) (Co- and, Ni-AGAO) exhibited 2.2 and 0.9% activities, respectively, of the original, Cu(2+)-enzyme (Cu-AGAO), but their K(m) values for amine substrate and, dioxygen were comparable. X-ray crystal structures of the Co- and Ni-AGAO, were solved at 2.0-1.8 A resolution. These structures revealed changes in, the metal coordination environment when compared to that of Cu-AGAO., However, the hydrogen-bonding network around the active site involving, metal-coordinating and noncoordinating water molecules was preserved. Upon, anaerobic mixing of the Cu-, Co-, and Ni-AGAO with amine substrate, the, 480 nm absorption band characteristic of the oxidized form of the, topaquinone cofactor (TPQ(ox)) disappeared rapidly (&lt; 6 ms), yielding the, aminoresorcinol form of the reduced cofactor (TPQ(amr)). In contrast to, the substrate-reduced Cu-AGAO, the semiquinone radical (TPQ(sq)) was not, detected in Co- and Ni-AGAO. Further, in the latter, TPQ(amr) reacted, reversibly with the product aldehyde to form a species with a lambda(max), at around 350 nm that was assigned as the neutral form of the product, Schiff base (TPQ(pim)). Introduction of dioxygen to the substrate-reduced, Co- and Ni-AGAO resulted in the formation of a TPQ-related intermediate, absorbing at around 360 nm, which was assigned to the neutral iminoquinone, form of the 2e(-)-oxidized cofactor (TPQ(imq)) and which decayed, concomitantly with the generation of TPQ(ox). The rate of TPQ(imq), formation and its subsequent decay in Co- and Ni-AGAO was slow when, compared to those of the corresponding reactions in Cu-AGAO. The low, catalytic activities of the metal-substituted enzymes are due to the, impaired efficiencies of the oxidative half-reaction in the catalytic, cycle of amine oxidation. On the basis of these results, we propose that, the native Cu(2+) ion has essential roles such as catalyzing the electron, transfer between TPQ(amr) and dioxygen, in part by providing a binding, site for 1e(-)- and 2e(-)-reduced dioxygen species to be efficiently, protonated and released and also preventing the back reaction between the, product aldehyde and TPQ(amr).
<StructureSection load='1iqx' size='340' side='right'caption='[[1iqx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iqx]] is a 2 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=1IQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQX 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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=1iqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqx OCA], [https://pdbe.org/1iqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iqx RCSB], [https://www.ebi.ac.uk/pdbsum/1iqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqx 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/iq/1iqx_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=1iqx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IQX 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 CO 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=1IQX OCA].
*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes., Kishishita S, Okajima T, Kim M, Yamaguchi H, Hirota S, Suzuki S, Kuroda S, Tanizawa K, Mure M, J Am Chem Soc. 2003 Jan 29;125(4):1041-55. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12537504 12537504]
[[Category: Amine oxidase (copper-containing)]]
[[Category: Arthrobacter globiformis]]
[[Category: Arthrobacter globiformis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hirota, S.]]
[[Category: Hirota S]]
[[Category: Kim, M.]]
[[Category: Kim M]]
[[Category: Kishishita, S.]]
[[Category: Kishishita S]]
[[Category: Kuroda, S.]]
[[Category: Kuroda S]]
[[Category: Mure, M.]]
[[Category: Mure M]]
[[Category: Okajima, T.]]
[[Category: Okajima T]]
[[Category: Suzuki, S.]]
[[Category: Suzuki S]]
[[Category: Tanizawa, K.]]
[[Category: Tanizawa K]]
[[Category: Yamaguchi, H.]]
[[Category: Yamaguchi H]]
[[Category: CO]]
[[Category: amine oxidase]]
[[Category: arthrobacter globiformis]]
[[Category: co(ii)]]
[[Category: cobalt]]
[[Category: copper]]
[[Category: oxidoreductase]]
[[Category: quinone cofactor]]
[[Category: tpq]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:35:27 2007''

Latest revision as of 09:02, 3 April 2024

CRYSTAL STRUCTURE OF COBALT-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMISCRYSTAL STRUCTURE OF COBALT-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS

Structural highlights

1iqx is a 2 chain structure with sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAOX_ARTGO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1iqx, resolution 2.00Å

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