2fnw
From Proteopedia
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| - | [[Image:2fnw.jpg|left|200px]]<br /><applet load="2fnw" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2fnw, resolution 1.40Å" /> | ||
| - | '''Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3'''<br /> | ||
| - | == | + | ==Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3== |
| + | <StructureSection load='2fnw' size='340' side='right'caption='[[2fnw]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2fnw]] is a 2 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=2FNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FNW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
| + | <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></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnw OCA], [https://pdbe.org/2fnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fnw RCSB], [https://www.ebi.ac.uk/pdbsum/2fnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fnw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/2fnw_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2fnw ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The triplet metal-to-ligand charge transfer ((3)MLCT) dynamics of two structurally characterized Re(I)(CO)(3)(phen)(HisX)-modified (phen = 1,10-phenanthroline; X = 83, 109) Pseudomonas aeruginosa azurins have been investigated by picosecond time-resolved infrared (TRIR) spectroscopy in aqueous (D(2)O) solution. The (3)MLCT relaxation dynamics exhibited by the two Re(I)-azurins are very different from those of the sensitizer [Re(I)(CO)(3)(phen)(im)](+) (im = imidazole). Whereas the Re(I)(CO)(3) intramolecular vibrational relaxation in Re(I)(CO)(3)(phen)(HisX)Az (4 ps) is similar to that of [Re(I)(CO)(3)(phen)(im)](+) (2 ps), the medium relaxation is much slower ( approximately 250 vs 9.5 ps); the 250-ps relaxation is attributable to reorientation of D(2)O molecules as well as structural reorganization of the rhenium chromophore and nearby polar amino acids in each of the modified proteins. | The triplet metal-to-ligand charge transfer ((3)MLCT) dynamics of two structurally characterized Re(I)(CO)(3)(phen)(HisX)-modified (phen = 1,10-phenanthroline; X = 83, 109) Pseudomonas aeruginosa azurins have been investigated by picosecond time-resolved infrared (TRIR) spectroscopy in aqueous (D(2)O) solution. The (3)MLCT relaxation dynamics exhibited by the two Re(I)-azurins are very different from those of the sensitizer [Re(I)(CO)(3)(phen)(im)](+) (im = imidazole). Whereas the Re(I)(CO)(3) intramolecular vibrational relaxation in Re(I)(CO)(3)(phen)(HisX)Az (4 ps) is similar to that of [Re(I)(CO)(3)(phen)(im)](+) (2 ps), the medium relaxation is much slower ( approximately 250 vs 9.5 ps); the 250-ps relaxation is attributable to reorientation of D(2)O molecules as well as structural reorganization of the rhenium chromophore and nearby polar amino acids in each of the modified proteins. | ||
| - | = | + | Excited-state dynamics of structurally characterized [ReI(CO)3(phen)(HisX)]+ (X = 83, 109) Pseudomonas aeruginosa azurins in aqueous solution.,Blanco-Rodriguez AM, Busby M, Gradinaru C, Crane BR, Di Bilio AJ, Matousek P, Towrie M, Leigh BS, Richards JH, Vlcek A Jr, Gray HB J Am Chem Soc. 2006 Apr 5;128(13):4365-70. PMID:16569013<ref>PMID:16569013</ref> |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2fnw" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Azurin 3D structures|Azurin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
| + | [[Category: Crane BR]] | ||
| + | [[Category: Gradinaru C]] | ||
Current revision
Pseudomonas aeruginosa E2Q/H83Q/M109H-azurin RE(PHEN)(CO)3
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