1ils

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(New page: 200px<br /><applet load="1ils" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ils, resolution 2.2&Aring;" /> '''X-RAY CRYSTAL STRUCTU...)
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[[Image:1ils.gif|left|200px]]<br /><applet load="1ils" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ils, resolution 2.2&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA'''<br />
 
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==Overview==
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==X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA==
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The blue copper protein azurin from Pseudomonas aeruginosa contains a, single Trp residue that is believed to be involved in the inducible, intramolecular electron transfer from a disulphide group to the copper, centre. This residue shows in fluorescence spectra the highest energy, emission of tryptophan-containing compounds at room temperature, which is, explained by its rigid and highly hydrophobic environment. In order to, investigate the role of the Trp residue in electron transfer and the, influence of its environment, two mutations (17S and F110S) were, introduced that were thought to increase the polarity and the mobility in, its environment. The crystal structures of these mutants were solved at, 2.2 A and 2.3 A resolution, respectively. These provide a structural basis, for the changes observed in fluorescence spectra compared with the, wild-type protein. We conclude from our results that these changes are not, caused by a change in the dynamics of the Trp residue itself, but, exclusively by an increased effective dielectric constant of the, microenvironment of Trp48 and by changes in mobility of the mutated, residues.
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<StructureSection load='1ils' size='340' side='right'caption='[[1ils]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ils]] 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=1ILS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILS 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]] 2.2&#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=NO3:NITRATE+ION'>NO3</scene></td></tr>
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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=1ils FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ils OCA], [https://pdbe.org/1ils PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ils RCSB], [https://www.ebi.ac.uk/pdbsum/1ils PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ils 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/il/1ils_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=1ils 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 blue copper protein azurin from Pseudomonas aeruginosa contains a single Trp residue that is believed to be involved in the inducible intramolecular electron transfer from a disulphide group to the copper centre. This residue shows in fluorescence spectra the highest energy emission of tryptophan-containing compounds at room temperature, which is explained by its rigid and highly hydrophobic environment. In order to investigate the role of the Trp residue in electron transfer and the influence of its environment, two mutations (17S and F110S) were introduced that were thought to increase the polarity and the mobility in its environment. The crystal structures of these mutants were solved at 2.2 A and 2.3 A resolution, respectively. These provide a structural basis for the changes observed in fluorescence spectra compared with the wild-type protein. We conclude from our results that these changes are not caused by a change in the dynamics of the Trp residue itself, but exclusively by an increased effective dielectric constant of the microenvironment of Trp48 and by changes in mobility of the mutated residues.
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==About this Structure==
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X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa.,Hammann C, Messerschmidt A, Huber R, Nar H, Gilardi G, Canters GW J Mol Biol. 1996 Jan 26;255(3):362-6. PMID:8568881<ref>PMID:8568881</ref>
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1ILS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU and NO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ILS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa., Hammann C, Messerschmidt A, Huber R, Nar H, Gilardi G, Canters GW, J Mol Biol. 1996 Jan 26;255(3):362-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8568881 8568881]
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</div>
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[[Category: Pseudomonas aeruginosa]]
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<div class="pdbe-citations 1ils" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Hammann, C.]]
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[[Category: Huber, R.]]
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[[Category: Messerschmidt, A.]]
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[[Category: Nar, H.]]
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[[Category: CU]]
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[[Category: NO3]]
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[[Category: electron transfer protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:29:24 2007''
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==See Also==
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*[[Azurin 3D structures|Azurin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Hammann C]]
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[[Category: Huber R]]
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[[Category: Messerschmidt A]]
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[[Category: Nar H]]

Current revision

X-RAY CRYSTAL STRUCTURE THE TWO SITE-SPECIFIC MUTANTS ILE7SER AND PHE110SER OF AZURIN FROM PSEUDOMONAS AERUGINOSA

PDB ID 1ils

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