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[[Image:2d5i.gif|left|200px]]


{{Structure
==The crystal structure of AzoR (Azo Reductase) from Escherichia coli==
|PDB= 2d5i |SIZE=350|CAPTION= <scene name='initialview01'>2d5i</scene>, resolution 2.20&Aring;
<StructureSection load='2d5i' size='340' side='right'caption='[[2d5i]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[2d5i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D5I FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Azobenzene_reductase Azobenzene reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.6 1.7.1.6] </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]] 2.2&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2d5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5i OCA], [https://pdbe.org/2d5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d5i RCSB], [https://www.ebi.ac.uk/pdbsum/2d5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d5i ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d5i OCA], [http://www.ebi.ac.uk/pdbsum/2d5i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d5i RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/AZOR_ECOLI AZOR_ECOLI] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes.<ref>PMID:2168383</ref>
 
== Evolutionary Conservation ==
'''The crystal structure of AzoR (Azo Reductase) from Escherichia coli'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d5/2d5i_consurf.spt"</scriptWhenChecked>
The crystal structure of AzoR (azoreductase) has been determined in complex with FMN for two different crystal forms at 1.8 and 2.2 A resolution. AzoR is an oxidoreductase isolated from Escherichia coli as a protein responsible for the degradation of azo compounds. This enzyme is an FMN-dependent NADH-azoreductase and catalyzes the reductive cleavage of azo groups by a ping-pong mechanism. The structure suggests that AzoR acts in a homodimeric state forming the two identical catalytic sites to which both monomers contribute. The structure revealed that each monomer of AzoR has a flavodoxin-like structure, without the explicit overall amino acid sequence homology. Superposition of the structures from the two different crystal forms revealed the conformational change and suggested a mechanism for accommodating substrates of different size. Furthermore, comparison of the active site structure with that of NQO1 complexed with substrates provides clues to the possible substrate-binding mechanism of AzoR.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
2D5I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5I OCA].  
</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=2d5i ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms., Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M, J Biol Chem. 2006 Jul 21;281(29):20567-76. Epub 2006 May 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16684776 16684776]
<references/>
[[Category: Azobenzene reductase]]
__TOC__
[[Category: Escherichia coli]]
</StructureSection>
[[Category: Single protein]]
[[Category: Escherichia coli K-12]]
[[Category: Ito, K.]]
[[Category: Large Structures]]
[[Category: Tanokura, M.]]
[[Category: Ito K]]
[[Category: azo reductase]]
[[Category: Tanokura M]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:36 2008''

Latest revision as of 13:46, 13 March 2024

The crystal structure of AzoR (Azo Reductase) from Escherichia coli

2d5i, resolution 2.20Å

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