4mfh: Difference between revisions
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==Crystal Structure of M121G Azurin== | |||
=== | <StructureSection load='4mfh' size='340' side='right' caption='[[4mfh]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mfh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MFH FirstGlance]. <br> | |||
</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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |||
<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=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | |||
<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=4mfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mfh RCSB], [http://www.ebi.ac.uk/pdbsum/4mfh PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Metal-sulfenate centers are known to play important roles in biology and yet only limited examples are known due to their instability and high reactivity. Herein we report a copper-sulfenate complex characterized in a protein environment, formed at the active site of a cavity mutant of an electron transfer protein, type 1 blue copper azurin. Reaction of hydrogen peroxide with Cu(I)-M121G azurin resulted in a species with strong visible absorptions at 350 and 452 nm and a relatively low electron paramagnetic resonance gz value of 2.169 in comparison with other normal type 2 copper centers. The presence of a side-on copper-sulfenate species is supported by resonance Raman spectroscopy, electrospray mass spectrometry using isotopically enriched hydrogen peroxide, and density functional theory calculations correlated to the experimental data. In contrast, the reaction with Cu(II)-M121G or Zn(II)-M121G azurin under the same conditions did not result in Cys oxidation or copper-sulfenate formation. Structural and computational studies strongly suggest that the secondary coordination sphere noncovalent interactions are critical in stabilizing this highly reactive species, which can further react with oxygen to form a sulfinate and then a sulfonate species, as demonstrated by mass spectrometry. Engineering the electron transfer protein azurin into an active copper enzyme that forms a copper-sulfenate center and demonstrating the importance of noncovalent secondary sphere interactions in stabilizing it constitute important contributions toward the understanding of metal-sulfenate species in biological systems. | |||
Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin.,Sieracki NA, Tian S, Hadt RG, Zhang JL, Woertink JS, Nilges MJ, Sun F, Solomon EI, Lu Y Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):924-9. doi: 10.1073/pnas.1316483111., Epub 2014 Jan 3. PMID:24390543<ref>PMID:24390543</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Azurin|Azurin]] | |||
[[Category: Lu, Y | == References == | ||
[[Category: Tian, S | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lu, Y]] | |||
[[Category: Tian, S]] | |||
[[Category: Electron transfer]] | [[Category: Electron transfer]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Greek key beta-barrel]] | [[Category: Greek key beta-barrel]] | ||
[[Category: Periplasmic]] | [[Category: Periplasmic]] | ||
Revision as of 19:27, 21 December 2014
Crystal Structure of M121G AzurinCrystal Structure of M121G Azurin
Structural highlights
Publication Abstract from PubMedMetal-sulfenate centers are known to play important roles in biology and yet only limited examples are known due to their instability and high reactivity. Herein we report a copper-sulfenate complex characterized in a protein environment, formed at the active site of a cavity mutant of an electron transfer protein, type 1 blue copper azurin. Reaction of hydrogen peroxide with Cu(I)-M121G azurin resulted in a species with strong visible absorptions at 350 and 452 nm and a relatively low electron paramagnetic resonance gz value of 2.169 in comparison with other normal type 2 copper centers. The presence of a side-on copper-sulfenate species is supported by resonance Raman spectroscopy, electrospray mass spectrometry using isotopically enriched hydrogen peroxide, and density functional theory calculations correlated to the experimental data. In contrast, the reaction with Cu(II)-M121G or Zn(II)-M121G azurin under the same conditions did not result in Cys oxidation or copper-sulfenate formation. Structural and computational studies strongly suggest that the secondary coordination sphere noncovalent interactions are critical in stabilizing this highly reactive species, which can further react with oxygen to form a sulfinate and then a sulfonate species, as demonstrated by mass spectrometry. Engineering the electron transfer protein azurin into an active copper enzyme that forms a copper-sulfenate center and demonstrating the importance of noncovalent secondary sphere interactions in stabilizing it constitute important contributions toward the understanding of metal-sulfenate species in biological systems. Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin.,Sieracki NA, Tian S, Hadt RG, Zhang JL, Woertink JS, Nilges MJ, Sun F, Solomon EI, Lu Y Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):924-9. doi: 10.1073/pnas.1316483111., Epub 2014 Jan 3. PMID:24390543[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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