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1e67

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[[Image:1e67.gif|left|200px]]
 
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{{Structure
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==Zn-Azurin from Pseudomonas aeruginosa==
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|PDB= 1e67 |SIZE=350|CAPTION= <scene name='initialview01'>1e67</scene>, resolution 2.14&Aring;
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<StructureSection load='1e67' size='340' side='right'caption='[[1e67]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+B'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+D'>AC4</scene> and <scene name='pdbsite=AC5:No3+Binding+Site+For+Chain+A'>AC5</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NO3:NITRATE ION'>NO3</scene>
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<table><tr><td colspan='2'>[[1e67]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E67 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.14&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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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=1e67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e67 OCA], [https://pdbe.org/1e67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e67 RCSB], [https://www.ebi.ac.uk/pdbsum/1e67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e67 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
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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/e6/1e67_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=1e67 ConSurf].
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<div style="clear:both"></div>
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'''ZN-AZURIN FROM PSEUDOMONAS AERUGINOSA'''
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==See Also==
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*[[Azurin 3D structures|Azurin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Azurin*, a by-product of heterologous expression of the gene encoding the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli, was characterized by chemical analysis and electrospray ionization mass spectrometry, and its structure determined by X-ray crystallography. It was shown that azurin* is native azurin with its copper atom replaced by zinc in the metal binding site. Zinc is probably incorporated in the apo-protein after its expression and transport into the periplasm. Holo-azurin can be reconstituted from azurin* by prolonged exposure of the protein to high copper ion concentrations or unfolding of the protein and refolding in the presence of copper ions. An X-ray crystallographic analysis of azurin* at 0.21-nm resolution revealed that the overall structure of azurin is not perturbed by the metal exchange. However, the geometry of the co-ordination sphere changes from trigonal bipyramidal in the case of copper azurin to distorted tetrahedral for the zinc protein. The copper ligand Met121 is no longer co-ordinated to zinc which adopts a position close to the carbonyl oxygen atom from residue Gly45. The polypeptide structure surrounding the metal site undergoes moderate reorganization upon zinc binding. The largest displacement observed is for the carbonyl oxygen from residue Gly45, which is involved in copper and zinc binding. It moves by 0.03 nm towards the zinc, thereby reducing its distance to the metal from 0.29 nm in the copper protein to 0.23 nm in the derivative.
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[[Category: Large Structures]]
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==About this Structure==
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1E67 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E67 OCA].
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==Reference==
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Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin., Nar H, Huber R, Messerschmidt A, Filippou AC, Barth M, Jaquinod M, van de Kamp M, Canters GW, Eur J Biochem. 1992 May 1;205(3):1123-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1576995 1576995]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Messerschmidt A]]
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[[Category: Messerschmidt, A.]]
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[[Category: Nar H]]
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[[Category: Nar, H.]]
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[[Category: NO3]]
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[[Category: ZN]]
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[[Category: electron transport(copper binding)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:24 2008''
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Current revision

Zn-Azurin from Pseudomonas aeruginosa

PDB ID 1e67

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