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Title: Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis

Abstract

We report multicopper oxidases (MCOs) represent a diverse family of enzymes that catalyze the oxidation of either an organic or a metal substrate with concomitant reduction of dioxygen to water. These enzymes contain variable numbers of cupredoxin domains, two, three or six per subunit, and rely on four copper ions, a single type I copper and three additional copper ions organized in a trinuclear cluster (TNC), with one type II and two type III copper ions, to catalyze the reaction. Here, two crystal structures and the enzymatic characterization of Marinithermus hydrothermalis MCO, a two-domain enzyme, are reported. This enzyme decolorizes Congo Red dye at 70°C in the presence of high halide concentrations and may therefore be useful in the detoxification of industrial waste that contains dyes. In two distinct crystal structures, MhMCO forms the trimers seen in other two-domain MCOs, but differs from these enzymes in that four trimers interact to create a dodecamer. This dodecamer of MhMCO forms a closed ball-like structure and has implications for the sequestration of bound divalent metal ions as well as substrate accessibility. In each subunit of the dodecameric structures, a Trp residue, Trp351, located between the type I and TNC sites exists inmore » two distinct conformations, consistent with a potential role in facilitating electron transfer in the enzyme.« less

Authors:
ORCiD logo [1];  [1];  [2];  [1]
+ Show Author Affiliations
  1. Indiana University School of Medicine, Indianapolis IN (United States)
  2. Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
National Institutes of Health (NIH); National Cancer Institute (NCI); USDOE Office of Science (SC), Basic Energy Sciences (BES); US Department of Education
OSTI Identifier:
1854592
Grant/Contract Number:  
AC02-06CH11357; ACB-12002; AGM-12006; P30GM138396; P015B180101-21
Resource Type:
Accepted Manuscript
Journal Name:
Acta Crystallographica. Section D. Structural Biology
Additional Journal Information:
Journal Volume: 77; Journal Issue: 10; Journal ID: ISSN 2059-7983
Publisher:
IUCr
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; crystal structure; dodecamers; laccases; multi-copper oxidases; thermophiles; Marinithermus hydrothermalis

Citation Formats

Paavola, Joseph L., Battistin, Umberto, Ogata, Craig M., and Georgiadis, Millie M. Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis. United States: N. p., 2021. Web. doi:10.1107/s205979832100944x.
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Paavola, Joseph L., Battistin, Umberto, Ogata, Craig M., & Georgiadis, Millie M. Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis. United States. https://doi.org/10.1107/s205979832100944x
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Paavola, Joseph L., Battistin, Umberto, Ogata, Craig M., and Georgiadis, Millie M. Wed . "Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis". United States. https://doi.org/10.1107/s205979832100944x. https://www.osti.gov/servlets/purl/1854592.
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@article{osti_1854592,
title = {Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis},
author = {Paavola, Joseph L. and Battistin, Umberto and Ogata, Craig M. and Georgiadis, Millie M.},
abstractNote = {We report multicopper oxidases (MCOs) represent a diverse family of enzymes that catalyze the oxidation of either an organic or a metal substrate with concomitant reduction of dioxygen to water. These enzymes contain variable numbers of cupredoxin domains, two, three or six per subunit, and rely on four copper ions, a single type I copper and three additional copper ions organized in a trinuclear cluster (TNC), with one type II and two type III copper ions, to catalyze the reaction. Here, two crystal structures and the enzymatic characterization of Marinithermus hydrothermalis MCO, a two-domain enzyme, are reported. This enzyme decolorizes Congo Red dye at 70°C in the presence of high halide concentrations and may therefore be useful in the detoxification of industrial waste that contains dyes. In two distinct crystal structures, MhMCO forms the trimers seen in other two-domain MCOs, but differs from these enzymes in that four trimers interact to create a dodecamer. This dodecamer of MhMCO forms a closed ball-like structure and has implications for the sequestration of bound divalent metal ions as well as substrate accessibility. In each subunit of the dodecameric structures, a Trp residue, Trp351, located between the type I and TNC sites exists in two distinct conformations, consistent with a potential role in facilitating electron transfer in the enzyme.},
doi = {10.1107/s205979832100944x},
journal = {Acta Crystallographica. Section D. Structural Biology},
number = 10,
volume = 77,
place = {United States},
year = {Wed Sep 29 00:00:00 EDT 2021},
month = {Wed Sep 29 00:00:00 EDT 2021}
}
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https://doi.org/10.1107/s205979832100944x
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