2fta

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{{Seed}}
 
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[[Image:2fta.png|left|200px]]
 
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==Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"==
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The line below this paragraph, containing "STRUCTURE_2fta", creates the "Structure Box" on the page.
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<StructureSection load='2fta' size='340' side='right'caption='[[2fta]], [[Resolution|resolution]] 1.61&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'>[[2fta]] 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=2FTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTA FirstGlance]. <br>
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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]] 1.61&#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=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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{{STRUCTURE_2fta| PDB=2fta | 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=2fta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fta OCA], [https://pdbe.org/2fta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fta RCSB], [https://www.ebi.ac.uk/pdbsum/2fta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fta 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/ft/2fta_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fta 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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The main active-site loop of the copper-binding protein azurin (a cupredoxin) has been shortened from C(112)TFPGH(117)SALM(121) to C(112)TPH(115)PFM(118) (the native loop from the cupredoxin amicyanin) and also to C(112)TPH(115)PM(117). The Cu(II) site structure is almost unaffected by shortening, as is that of the Cu(I) center at alkaline pH in the variant with the C(112)TPH(115)PM(117) loop sequence. Subtle spectroscopic differences due to alterations in the spin density distribution at the Cu(II) site can be attributed mainly to changes in the hydrogen-bonding pattern. Electron transfer is almost unaffected by the introduction of the C(112)TPH(115)PFM(118) loop, but removal of the Phe residue has a sizable effect on reactivity, probably because of diminished homodimer formation. At mildly acidic pH values, the His-115 ligand protonates and dissociates from the cuprous ion, an effect that has a dramatic influence on the reactivity of cupredoxins. These studies demonstrate that the amicyanin loop adopts a conformation identical to that found in the native protein when introduced into azurin, that a shorter than naturally occurring C-terminal active-site loop can support a functional T1 copper site, that CTPHPM is the minimal loop length required for binding this ubiquitous electron transfer center, and that the length and sequence of a metal-binding loop regulates a range of structural and functional features of the active site of a metalloprotein.
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===Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"===
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Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin.,Li C, Yanagisawa S, Martins BM, Messerschmidt A, Banfield MJ, Dennison C Proc Natl Acad Sci U S A. 2006 May 9;103(19):7258-63. Epub 2006 May 1. PMID:16651527<ref>PMID:16651527</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 2fta" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16651527}}, 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 16651527 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16651527}}
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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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2FTA 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=2FTA OCA].
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==Reference==
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Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin., Li C, Yanagisawa S, Martins BM, Messerschmidt A, Banfield MJ, Dennison C, Proc Natl Acad Sci U S A. 2006 May 9;103(19):7258-63. Epub 2006 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16651527 16651527]
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Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip., Nar H, Messerschmidt A, Huber R, van de Kamp M, Canters GW, J Mol Biol. 1991 Oct 5;221(3):765-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1942029 1942029]
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Loop-contraction mutagenesis of type 1 copper sites., Yanagisawa S, Dennison C, J Am Chem Soc. 2004 Dec 8;126(48):15711-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15571393 15571393]
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Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus., Romero A, Nar H, Huber R, Messerschmidt A, Kalverda AP, Canters GW, Durley R, Mathews FS, J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8120896 8120896]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Banfield MJ]]
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[[Category: Banfield, M J.]]
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[[Category: Blue copper-binding protein]]
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[[Category: Greek-key beta-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:26:05 2008''
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Current revision

Structure of Cu(II)azurin with the metal-binding loop sequence "CTFPGHSALM" replaced with "CTPHPFM"

PDB ID 2fta

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