6mjs: Difference between revisions

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'''Unreleased structure'''


The entry 6mjs is ON HOLD  until Paper Publication
==Azurin 122W/124W/126Re==
<StructureSection load='6mjs' size='340' side='right'caption='[[6mjs]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6mjs]] is a 4 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=6MJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MJS 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]] 1.85&#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=6mjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mjs OCA], [https://pdbe.org/6mjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mjs RCSB], [https://www.ebi.ac.uk/pdbsum/6mjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mjs 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 ==
We have constructed and structurally characterized a Pseudomonas aeruginosa azurin mutant Re126WWCu(I) , where two adjacent tryptophan residues (W124 and W122, indole separation 3.6-4.1 A) are inserted between the Cu(I) center and a Re photosensitizer coordinated to the imidazole of H126 (Re(I)(H126)(CO)3(4,7-dimethyl-1,10-phenanthroline)(+)). Cu(I) oxidation by the photoexcited Re label (*Re) 22.9 A away proceeds with a approximately 70 ns time constant, similar to that of a single-tryptophan mutant ( approximately 40 ns) with a 19.4 A Re-Cu distance. Time-resolved spectroscopy (luminescence, visible and IR absorption) revealed two rapid reversible electron transfer steps, W124 --&gt; *Re (400-475 ps, K 1 congruent with 3.5-4) and W122 --&gt; W124(*+) (7-9 ns, K 2 congruent with 0.55-0.75), followed by a rate-determining (70-90 ns) Cu(I) oxidation by W122(*+) ca. 11 A away. The photocycle is completed by 120 mus recombination. No photochemical Cu(I) oxidation was observed in Re126FWCu(I) , whereas in Re126WFCu(I) , the photocycle is restricted to the ReH126W124 unit and Cu(I) remains isolated. QM/MM/MD simulations of Re126WWCu(I) indicate that indole solvation changes through the hopping process and W124 --&gt; *Re electron transfer is accompanied by water fluctuations that tighten W124 solvation. Our finding that multistep tunneling (hopping) confers a approximately 9000-fold advantage over single-step tunneling in the double-tryptophan protein supports the proposal that hole-hopping through tryptophan/tyrosine chains protects enzymes from oxidative damage.


Authors: Takematsu, K., Zalis, S., Gray, H.B., Vlcek, A., Winkler, J.R., Williamson, H., Kaiser, J.T., Heyda, J., Hollas, D.
Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein.,Takematsu K, Williamson HR, Nikolovski P, Kaiser JT, Sheng Y, Pospisil P, Towrie M, Heyda J, Hollas D, Zalis S, Gray HB, Vlcek A, Winkler JR ACS Cent Sci. 2019 Jan 23;5(1):192-200. doi: 10.1021/acscentsci.8b00882. Epub, 2019 Jan 7. PMID:30693338<ref>PMID:30693338</ref>


Description: Azurin 122W/124W/126Re
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hollas, D]]
<div class="pdbe-citations 6mjs" style="background-color:#fffaf0;"></div>
[[Category: Williamson, H]]
 
[[Category: Heyda, J]]
==See Also==
[[Category: Gray, H.B]]
*[[Azurin 3D structures|Azurin 3D structures]]
[[Category: Kaiser, J.T]]
== References ==
[[Category: Vlcek, A]]
<references/>
[[Category: Takematsu, K]]
__TOC__
[[Category: Zalis, S]]
</StructureSection>
[[Category: Winkler, J.R]]
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Gray HB]]
[[Category: Heyda J]]
[[Category: Hollas D]]
[[Category: Kaiser JT]]
[[Category: Takematsu K]]
[[Category: Vlcek A]]
[[Category: Williamson H]]
[[Category: Winkler JR]]
[[Category: Zalis S]]

Latest revision as of 08:25, 21 November 2024

Azurin 122W/124W/126ReAzurin 122W/124W/126Re

Structural highlights

6mjs is a 4 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase.

Publication Abstract from PubMed

We have constructed and structurally characterized a Pseudomonas aeruginosa azurin mutant Re126WWCu(I) , where two adjacent tryptophan residues (W124 and W122, indole separation 3.6-4.1 A) are inserted between the Cu(I) center and a Re photosensitizer coordinated to the imidazole of H126 (Re(I)(H126)(CO)3(4,7-dimethyl-1,10-phenanthroline)(+)). Cu(I) oxidation by the photoexcited Re label (*Re) 22.9 A away proceeds with a approximately 70 ns time constant, similar to that of a single-tryptophan mutant ( approximately 40 ns) with a 19.4 A Re-Cu distance. Time-resolved spectroscopy (luminescence, visible and IR absorption) revealed two rapid reversible electron transfer steps, W124 --> *Re (400-475 ps, K 1 congruent with 3.5-4) and W122 --> W124(*+) (7-9 ns, K 2 congruent with 0.55-0.75), followed by a rate-determining (70-90 ns) Cu(I) oxidation by W122(*+) ca. 11 A away. The photocycle is completed by 120 mus recombination. No photochemical Cu(I) oxidation was observed in Re126FWCu(I) , whereas in Re126WFCu(I) , the photocycle is restricted to the ReH126W124 unit and Cu(I) remains isolated. QM/MM/MD simulations of Re126WWCu(I) indicate that indole solvation changes through the hopping process and W124 --> *Re electron transfer is accompanied by water fluctuations that tighten W124 solvation. Our finding that multistep tunneling (hopping) confers a approximately 9000-fold advantage over single-step tunneling in the double-tryptophan protein supports the proposal that hole-hopping through tryptophan/tyrosine chains protects enzymes from oxidative damage.

Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein.,Takematsu K, Williamson HR, Nikolovski P, Kaiser JT, Sheng Y, Pospisil P, Towrie M, Heyda J, Hollas D, Zalis S, Gray HB, Vlcek A, Winkler JR ACS Cent Sci. 2019 Jan 23;5(1):192-200. doi: 10.1021/acscentsci.8b00882. Epub, 2019 Jan 7. PMID:30693338[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Takematsu K, Williamson HR, Nikolovski P, Kaiser JT, Sheng Y, Pospisil P, Towrie M, Heyda J, Hollas D, Zalis S, Gray HB, Vlcek A, Winkler JR. Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein. ACS Cent Sci. 2019 Jan 23;5(1):192-200. doi: 10.1021/acscentsci.8b00882. Epub, 2019 Jan 7. PMID:30693338 doi:http://dx.doi.org/10.1021/acscentsci.8b00882

6mjs, resolution 1.85Å

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