View source for 3ibo


==Pseudomonas aeruginosa E2Q/H83Q/T126H-azurin RE(PHEN)(CO)3==
<StructureSection load='3ibo' size='340' side='right'caption='[[3ibo]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ibo]] 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=3IBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IBO 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]] 1.45&#8491;</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=3ibo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ibo OCA], [https://pdbe.org/3ibo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ibo RCSB], [https://www.ebi.ac.uk/pdbsum/3ibo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ibo 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/ib/3ibo_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=3ibo ConSurf].
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== Publication Abstract from PubMed ==
Photoinduced relaxation processes of five structurally characterized Pseudomonas aeruginosa Re(I)(CO)(3)(alpha-diimine)(HisX) (X = 83, 107, 109, 124, 126)Cu(II) azurins have been investigated by time-resolved (ps-ns) IR spectroscopy and emission spectroscopy. Crystal structures reveal the presence of Re-azurin dimers and trimers that in two cases (X = 107, 124) involve van der Waals interactions between interdigitated diimine aromatic rings. Time-dependent emission anisotropy measurements confirm that the proteins aggregate in mM solutions (D(2)O, KP(i) buffer, pD = 7.1). Excited-state DFT calculations show that extensive charge redistribution in the Re(I)(CO)(3) --&gt; diimine (3)MLCT state occurs: excitation of this (3)MLCT state triggers several relaxation processes in Re-azurins whose kinetics strongly depend on the location of the metallolabel on the protein surface. Relaxation is manifested by dynamic blue shifts of excited-state nu(CO) IR bands that occur with triexponential kinetics: intramolecular vibrational redistribution together with vibrational and solvent relaxation give rise to subps, approximately 2, and 8-20 ps components, while the approximately 10(2) ps kinetics are attributed to displacement (reorientation) of the Re(I)(CO)(3)(phen)(im) unit relative to the peptide chain, which optimizes Coulombic interactions of the Re(I) excited-state electron density with solvated peptide groups. Evidence also suggests that additional segmental movements of Re-bearing beta-strands occur without perturbing the reaction field or interactions with the peptide. Our work demonstrates that time-resolved IR spectroscopy and emission anisotropy of Re(I) carbonyl-diimine complexes are powerful probes of molecular dynamics at or around the surfaces of proteins and protein-protein interfacial regions.

Relaxation dynamics of Pseudomonas aeruginosa Re(I)(CO)3(alpha-diimine)(HisX)+ (X = 83, 107, 109, 124, 126)Cu(II) azurins.,Blanco-Rodriguez AM, Busby M, Ronayne K, Towrie M, Gradinaru C, Sudhamsu J, Sykora J, Hof M, Zalis S, Di Bilio AJ, Crane BR, Gray HB, Vlcek A Jr J Am Chem Soc. 2009 Aug 26;131(33):11788-800. PMID:19639996<ref>PMID:19639996</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ibo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Azurin 3D structures|Azurin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Crane BR]]
[[Category: Gradinaru C]]
[[Category: Sudhamsu J]]