1wzd: Difference between revisions

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New page: left|200px<br /><applet load="1wzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wzd, resolution 1.35Å" /> '''Crystal Structure Of...
 
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[[Image:1wzd.gif|left|200px]]<br /><applet load="1wzd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wzd, resolution 1.35&Aring;" />
'''Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase'''<br />


==Overview==
==Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase==
Protein-to-protein electron transfer (ET) is a critical process in, biological chemistry for which fundamental understanding is expected to, provide a wealth of applications in biotechnology. Investigations of, protein-protein ET systems in reductive activation of artificial cofactors, introduced into proteins remains particularly challenging because of the, complexity of interactions between the cofactor and the system, contributing to ET. In this work, we construct an artificial, protein-protein ET system, using heme oxygenase (HO), which is known to, catalyze the conversion of heme to biliverdin. HO uses electrons provided, from NADPH/cytochrome P450 reductase (CPR) through protein-protein complex, formation during the enzymatic reaction. We report that a, Fe(III)(Schiff-base), in the place of the active-site heme prosthetic, group of HO, can be reduced by NADPH/CPR. The crystal structure of the, Fe(10-CH(2)CH(2)COOH-Schiff-base).HO composite indicates the presence of a, hydrogen bond between the propionic acid carboxyl group and Arg-177 of HO., Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold, faster than that of Fe(Schiff-base).HO, although the redox potential of, Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that, of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen, electrode. This work describes a synthetic metal complex activated by, means of a protein-protein ET system, which has not previously been, reported. Moreover, the result suggests the importance of the hydrogen, bond for the ET reaction of HO. Our Fe(Schiff-base).HO composite model, system may provide insights with regard to design of ET biosystems for, sensors, catalysts, and electronics devices.
<StructureSection load='1wzd' size='340' side='right'caption='[[1wzd]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wzd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZD 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOK:[[2,2-[4-CARBOXYETHYL-1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOK</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=1wzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzd OCA], [https://pdbe.org/1wzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzd RCSB], [https://www.ebi.ac.uk/pdbsum/1wzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q54AI1_CORDP Q54AI1_CORDP]
== 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/wz/1wzd_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=1wzd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1WZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae] with SO4, YOK and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WZD OCA].
*[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Design of metal cofactors activated by a protein-protein electron transfer system., Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y, Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9416-21. Epub 2006 Jun 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16769893 16769893]
[[Category: Corynebacterium diphtheriae]]
[[Category: Corynebacterium diphtheriae]]
[[Category: Heme oxygenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Ikeda-Saito M]]
[[Category: Ikeda-Saito, M.]]
[[Category: Ueno T]]
[[Category: Ueno, T.]]
[[Category: Unno M]]
[[Category: Unno, M.]]
[[Category: Watanabe Y]]
[[Category: Watanabe, Y.]]
[[Category: Yokoi N]]
[[Category: Yokoi, N.]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: YOK]]
[[Category: artificial metalloprotein]]
[[Category: electron-transfer]]
[[Category: heme oxygenase]]
[[Category: metal]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:07:07 2007''

Latest revision as of 16:35, 13 March 2024

Crystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenaseCrystal Structure Of An Artificial Metalloprotein: Fe(10-CH2CH2COOH-Salophen)/Wild Type Heme oxygenase

Structural highlights

1wzd is a 2 chain structure with sequence from Corynebacterium diphtheriae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.35Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q54AI1_CORDP

Evolutionary Conservation

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

See Also

1wzd, resolution 1.35Å

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