4JKN

Mercury Metallated Pseudomonas aeruginosa Azurin at 1.54 A

Summary for 4JKN

• Entry DOI: 10.2210/pdb4jkn/pdb
• Related: 3UGE
• Descriptor: Azurin, MERCURY (II) ION, NITRATE ION, ... (5 entities in total)
• Functional Keywords: electron transport, mercury metallation
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm: P00282
• Total number of polymer chains: 4
• Total formula weight: 57380.24

Authors

Zampino, A.P.,Masters, F.M.,Bladholm, E.L.,Berry, S.B.,Panzner, M.J.,Ziegler, C.J. (deposition date: 2013-03-10, release date: 2014-02-19, Last modification date: 2024-11-27)

Primary citation

Zampino, A.P.,Masters, F.M.,Bladholm, E.L.,Panzner, M.J.,Berry, S.M.,Leeper, T.C.,Ziegler, C.J.
Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity.
J.Inorg.Biochem., 141:152-160, 2014

PubMed Abstract: Mercury(II) metallation of Pseudomonas aeruginosa azurin has been characterized structurally and biochemically. The X-ray crystal structure at 1.5Å 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.

PubMed: 25265377
DOI: 10.1016/j.jinorgbio.2014.09.003

Experimental method

X-RAY DIFFRACTION (1.536 Å)