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4jkn

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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.
[[http://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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Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5A of mercury(II) metallated azurin confirms the coordination of mercury at the copper binding active site and a second surface site. These findings are further validated by NMR, Matrix-assisted laser desorption/ionization spectrometry (MALDI), and UV-visible spectroscopic methods indicating copper displacement from the wild-type protein. Bioinformatic analysis has identified homologous human protein domains computationally, and compared them to the structure of azurin, providing a model for human mercury interactions. Study of the mercury-azurin adduct, in combination with other known examples of protein-heavy metal interactions, could provide further insight into the chemical mechanisms of toxicological interactions, leading toward a global understanding of the biological speciation of toxic heavy metals.
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Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity.,Zampino AP, Masters FM, Bladholm EL, Panzner MJ, Berry SM, Leeper TC, Ziegler CJ J Inorg Biochem. 2014 Dec;141:152-60. doi: 10.1016/j.jinorgbio.2014.09.003. Epub , 2014 Sep 16. PMID:25265377<ref>PMID:25265377</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>
==See Also==
==See Also==
*[[Azurin|Azurin]]
*[[Azurin|Azurin]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 10:11, 7 February 2015

Mercury Metallated Pseudomonas aeruginosa Azurin at 1.54 A

4jkn, resolution 1.54Å

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