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4k9j

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==Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant==
==Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant==
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<StructureSection load='4k9j' size='340' side='right' caption='[[4k9j]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='4k9j' size='340' side='right'caption='[[4k9j]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4k9j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K9J FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=REQ:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REQ</scene></td></tr>
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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]] 1.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4azu|4azu]]</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=REQ:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REQ</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k9j RCSB], [http://www.ebi.ac.uk/pdbsum/4k9j PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.
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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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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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==See Also==
==See Also==
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*[[Azurin|Azurin]]
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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__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pseae]]
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[[Category: Large Structures]]
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[[Category: Blanco-Rodriguez, A M]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Clark, I P]]
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[[Category: Blanco-Rodriguez AM]]
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[[Category: Gray, H B]]
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[[Category: Clark IP]]
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[[Category: Jr, A Vlcek]]
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[[Category: Gray HB]]
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[[Category: Kaiser, J T]]
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[[Category: Kaiser JT]]
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[[Category: Nikolovski, P]]
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[[Category: Nikolovski P]]
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[[Category: Sokolova, L]]
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[[Category: Sokolova L]]
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[[Category: Takematsu, K]]
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[[Category: Takematsu K]]
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[[Category: Towrie, M]]
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[[Category: Towrie M]]
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[[Category: Williamson, H R]]
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[[Category: Vlcek Jr A]]
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[[Category: Winkler, J R]]
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[[Category: Williamson HR]]
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[[Category: Electron transport]]
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[[Category: Winkler JR]]
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[[Category: Rhenium]]
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Current revision

Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant

PDB ID 4k9j

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