View source for 4k9j


==Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant==
<StructureSection load='4k9j' size='340' side='right'caption='[[4k9j]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4k9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K9J 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]] 1.7&#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=4k9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9j OCA], [https://pdbe.org/4k9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k9j RCSB], [https://www.ebi.ac.uk/pdbsum/4k9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k9j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Re126W122CuI Pseudomonas aeruginosa azurin incorporates three redox sites, ReI(CO)3(4,7-dimethyl-1,10-phenanthroline) covalently bound at H126, the W122 indole side chain, and CuI, which are well separated in the protein fold: Re-W122(indole) = 13.1 A; dmp-W122(indole) = 10.0 A, Re-Cu = 25.6 A. In view of the long intramolecular Re-Cu distance, it is surprising that CuI is oxidized in less than 50 ns after near-UV excitation of the Re chromophore. Back electron transfer (BET) regenerating CuI and ground-state ReI takes much longer (220 ns and 6 us). We show that these ET reactions occur in protein dimers, (Re126W122CuI)2, which are in equilibrium with unreactive monomers. In support of this interpretation, ET yields and kinetics are concentration-dependent and solution mass spectrometry (LILBID-MS) confirms the presence of a broad oligomer distribution with prevalent monomers and dimers; in the crystal structure, two Re126W122CuII molecules are oriented in such a way that the redox cofactors Re(dmp) and W122-indole belonging to different monomers are located at a protein-protein interface (//), where the intermolecular ET-relevant distances (Re-W122(indole) = 6.9 A, dmp-W122(indole) = 3.5 A, and Re-Cu = 14.0 A) are much shorter than intramolecular ones. We propose that forward ET is accelerated by intermolecular electron hopping through a surface tryptophan: *Re//&lt;-W122&lt;-CuI; our kinetics analysis indicates that an equilibrium (K = 0.8-0.9) between *Re and charge-separated Re(dmp*-)(W122*+), which is established in a few ns, stores part of the excitation energy. The second ET step, intramolecular CuI oxidation, CuI-&gt;W122*+, occurs in 30 ns. The system is well coupled for forward ET but not for ReI(dmp*-)-&gt;CuII BET. Our work on interfacial electron hopping in (Re126W122CuI)2 sheds new light on redox-unit placements required for functional long-range charge separation in protein complexes.

Tryptophan-accelerated electron flow across a protein-protein interface.,Takematsu K, Williamson H, Blanco-Rodriguez AM, Sokolova L, Nikolovski P, Kaiser JT, Towrie M, Clark IP, Vlcek A, Winkler JR, Gray HB J Am Chem Soc. 2013 Sep 13. PMID:24032375<ref>PMID:24032375</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4k9j" style="background-color:#fffaf0;"></div>

==See Also==
*[[Azurin 3D structures|Azurin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Blanco-Rodriguez AM]]
[[Category: Clark IP]]
[[Category: Gray HB]]
[[Category: Kaiser JT]]
[[Category: Nikolovski P]]
[[Category: Sokolova L]]
[[Category: Takematsu K]]
[[Category: Towrie M]]
[[Category: Vlcek Jr A]]
[[Category: Williamson HR]]
[[Category: Winkler JR]]