X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins Export

@article{citeulike:4236411, abstract = {A multi-copper protein with two cupredoxin-like domains was identified from our in-house metagenomic database. The recombinant protein, mgLAC, contained four copper ions/subunits, oxidized various phenolic and non-phenolic substrates, and had spectroscopic properties similar to common laccases. X-ray structure analysis revealed a homotrimeric architecture for this enzyme, which resembles nitrite reductase (NIR). However, a difference in copper coordination was found at the domain interface. mgLAC contains a T2/T3 tri-nuclear copper cluster at this site, whereas a mononuclear T2 copper occupies this position in NIR. The trimer is thus an essential part of the architecture of two-domain multi-copper proteins, and mgLAC may be an evolutionary precursor of NIR.}, author = {Komori, Hirofumi and Miyazaki, Kentaro and Higuchi, Yoshiki}, citeulike-article-id = {4236411}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.febslet.2009.03.008}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0014579309001847}, day = {11}, doi = {10.1016/j.febslet.2009.03.008}, issn = {00145793}, journal = {FEBS Letters}, keywords = {domain\_combination, enzyme, experiment, structure, subunit}, month = {March}, posted-at = {2009-03-30 11:41:46}, priority = {2}, title = {X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins}, url = {http://dx.doi.org/10.1016/j.febslet.2009.03.008}, year = {2009} }

TY - JOUR ID - citeulike:4236411 L3 - citeulike-article-id:4236411 N2 - A multi-copper protein with two cupredoxin-like domains was identified from our in-house metagenomic database. The recombinant protein, mgLAC, contained four copper ions/subunits, oxidized various phenolic and non-phenolic substrates, and had spectroscopic properties similar to common laccases. X-ray structure analysis revealed a homotrimeric architecture for this enzyme, which resembles nitrite reductase (NIR). However, a difference in copper coordination was found at the domain interface. mgLAC contains a T2/T3 tri-nuclear copper cluster at this site, whereas a mononuclear T2 copper occupies this position in NIR. The trimer is thus an essential part of the architecture of two-domain multi-copper proteins, and mgLAC may be an evolutionary precursor of NIR. JF - FEBS Letters SN - 00145793 TI - X-ray structure of a two-domain type laccase: A missing link in the evolution of multi-copper proteins KW - domain_combination KW - enzyme KW - experiment KW - structure KW - subunit AU - Komori, Hirofumi AU - Miyazaki, Kentaro AU - Higuchi, Yoshiki PY - 2009/03/11/ UR - http://dx.doi.org/10.1016/j.febslet.2009.03.008 ER -