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3fq2

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{{Seed}}
 
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[[Image:3fq2.png|left|200px]]
 
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==Azurin C112D/M121F==
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The line below this paragraph, containing "STRUCTURE_3fq2", creates the "Structure Box" on the page.
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<StructureSection load='3fq2' size='340' side='right'caption='[[3fq2]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fq2]] is a 1 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=3FQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FQ2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.91&#8491;</td></tr>
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<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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_3fq2| PDB=3fq2 | SCENE= }}
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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=3fq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fq2 OCA], [https://pdbe.org/3fq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3fq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fq2 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/fq/3fq2_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=3fq2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Copper proteins play key roles in biological processes such as electron transfer and dioxygen activation; the active site of each of these proteins is classified as either type 1, 2, or 3, depending on its optical and electron paramagnetic resonance properties. We have built a new type of site that we call "type zero copper" by incorporating leucine, isoleucine, or phenylalanine in place of methionine at position 121 in C112D Pseudomonas aeruginosa azurin. X-ray crystallographic analysis shows that these sites adopt distorted tetrahedral geometries, with an unusually short Cu-O(G45 carbonyl) bond (2.35-2.55 A). Relatively weak absorption near 800 nm and narrow parallel hyperfine splittings in EPR spectra are the spectroscopic signatures of type zero copper. Copper K-edge x-ray absorption spectra suggest elevated Cu(II) 4p character in the d-electron ground state. Cyclic voltammetric experiments demonstrate that the electron transfer reactivities of type zero azurins are enhanced relative to that of the corresponding type 2 (C112D) protein.
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===Azurin C112D/M121F===
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Type Zero Copper Proteins.,Lancaster KM, Debeer George S, Yokoyama K, Richards JH, Gray HB Nat Chem. 2009 Dec 1;1(9):711-715. PMID:20305734<ref>PMID:20305734</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3fq2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20305734}}, adds the Publication Abstract to the page
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*[[Azurin 3D structures|Azurin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20305734 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20305734}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3FQ2 is a 1 chain structure with 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=3FQ2 OCA].
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==Reference==
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<ref group="xtra">PMID:20305734</ref><references group="xtra"/>
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Gray, H B.]]
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[[Category: Gray HB]]
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[[Category: Lancaster, K M.]]
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[[Category: Lancaster KM]]
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[[Category: Copper]]
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[[Category: Copper binding]]
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[[Category: Electron transport]]
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[[Category: Metal-binding]]
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[[Category: Periplasm]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 08:57:36 2010''
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Current revision

Azurin C112D/M121F

PDB ID 3fq2

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