7tc5: Difference between revisions
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==All Phe-Azurin variant - F15Y== | ==All Phe-Azurin variant - F15Y== | ||
<StructureSection load='7tc5' size='340' side='right'caption='[[7tc5]]' scene=''> | <StructureSection load='7tc5' size='340' side='right'caption='[[7tc5]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TC5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tc5]] 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=7TC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TC5 FirstGlance]. <br> | ||
</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=7tc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tc5 OCA], [https://pdbe.org/7tc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tc5 RCSB], [https://www.ebi.ac.uk/pdbsum/7tc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tc5 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=7tc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tc5 OCA], [https://pdbe.org/7tc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tc5 RCSB], [https://www.ebi.ac.uk/pdbsum/7tc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tc5 ProSAT]</span></td></tr> | |||
</table> | </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 == | |||
The interplay between the primary and secondary coordination spheres in biological metal sites plays an essential role in controlling their properties. Some of the clearest examples of this are from copper sites in blue and purple copper proteins. Many such proteins contain methionine (Met) in the primary coordination sphere as a weakly bound ligand to Cu. While the effects of replacing the coordinated Met are understood, less so is the importance of its second-sphere interactions. In this combined informatics and experimental study, we first present a bioinformatics investigation of the second-sphere environments in biological Met-Cu motifs. The most common interaction is between the Met-CH3 and the pi-face of a phenylalanine (Phe) (81% of surveyed structures), tyrosine (Tyr) (11%), and tryptophan (Trp) (8%). In most cases, the Met-CH3 also forms a contact with a pi-face of one of a Cu-ligating histidine-imidazole. Such interactions are widely distributed in different Cu proteins. Second, to explore the impact of the second-sphere interactions of Met, a series of artificial Pseudomonas aeruginosa azurin proteins were produced where the native Phe15 was replaced with Tyr or Trp. The proteins were characterized using optical and magnetic resonance spectroscopies, X-ray diffraction, electrochemistry, and an investigation of the time-resolved electron-transfer kinetics of photosensitizer-modified proteins. The influence of the Cu-Met-Aro interaction on azurin's physical properties is subtle, and the hallmarks of the azurin blue copper site are maintained. In the Phe15Trp variant, the mutation to Phe15 induces changes in Cu properties that are comparable to replacement of the weak Met ligand. The broader impacts of these widely distributed interactions are discussed. | |||
The Impact of Second Coordination Sphere Methionine-Aromatic Interactions in Copper Proteins.,Fedoretz-Maxwell BP, Shin CH, MacNeil GA, Worrall LJ, Park R, Strynadka NCJ, Walsby CJ, Warren JJ Inorg Chem. 2022 Apr 11;61(14):5563-5571. doi: 10.1021/acs.inorgchem.2c00030., Epub 2022 Mar 29. PMID:35347989<ref>PMID:35347989</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7tc5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Azurin 3D structures|Azurin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pseudomonas aeruginosa]] | |||
[[Category: Fedoretz-Maxwell BP]] | [[Category: Fedoretz-Maxwell BP]] | ||
[[Category: Strynadka NCJ]] | [[Category: Strynadka NCJ]] | ||
[[Category: Warren JJ]] | [[Category: Warren JJ]] | ||
[[Category: Worrall LJ]] | [[Category: Worrall LJ]] | ||
Latest revision as of 20:03, 18 October 2023
All Phe-Azurin variant - F15YAll Phe-Azurin variant - F15Y
Structural highlights
FunctionAZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Publication Abstract from PubMedThe interplay between the primary and secondary coordination spheres in biological metal sites plays an essential role in controlling their properties. Some of the clearest examples of this are from copper sites in blue and purple copper proteins. Many such proteins contain methionine (Met) in the primary coordination sphere as a weakly bound ligand to Cu. While the effects of replacing the coordinated Met are understood, less so is the importance of its second-sphere interactions. In this combined informatics and experimental study, we first present a bioinformatics investigation of the second-sphere environments in biological Met-Cu motifs. The most common interaction is between the Met-CH3 and the pi-face of a phenylalanine (Phe) (81% of surveyed structures), tyrosine (Tyr) (11%), and tryptophan (Trp) (8%). In most cases, the Met-CH3 also forms a contact with a pi-face of one of a Cu-ligating histidine-imidazole. Such interactions are widely distributed in different Cu proteins. Second, to explore the impact of the second-sphere interactions of Met, a series of artificial Pseudomonas aeruginosa azurin proteins were produced where the native Phe15 was replaced with Tyr or Trp. The proteins were characterized using optical and magnetic resonance spectroscopies, X-ray diffraction, electrochemistry, and an investigation of the time-resolved electron-transfer kinetics of photosensitizer-modified proteins. The influence of the Cu-Met-Aro interaction on azurin's physical properties is subtle, and the hallmarks of the azurin blue copper site are maintained. In the Phe15Trp variant, the mutation to Phe15 induces changes in Cu properties that are comparable to replacement of the weak Met ligand. The broader impacts of these widely distributed interactions are discussed. The Impact of Second Coordination Sphere Methionine-Aromatic Interactions in Copper Proteins.,Fedoretz-Maxwell BP, Shin CH, MacNeil GA, Worrall LJ, Park R, Strynadka NCJ, Walsby CJ, Warren JJ Inorg Chem. 2022 Apr 11;61(14):5563-5571. doi: 10.1021/acs.inorgchem.2c00030., Epub 2022 Mar 29. PMID:35347989[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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