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. 2015 Jul 17;8:101. doi: 10.1186/s13068-015-0284-1

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© Frommhagen et al. 2015

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Structural model of MtLPMO9A. a Structural model of MtLPMO9A generated using the available template structure of TtPMO1 from Thielavia terrestris (PDB-id: 3eii) [29]. The divalent metal ion (orange) in the flat face is coordinated by two histidines (His1 and His68; blue) and one tyrosine (Tyr153, magenta), which is typical for LPMOs belonging to subgroup AA9 of the CAZy database [30]. Compared to TtPMO1, Tyr191 is replaced by Asn191 in the flat face. Two disulfide bridges, Cys126–Cys208 and Cys38–Cys156, are conserved and expected to be crucial for the thermotolerance of MtLPMO9A. b Sequence alignment of MtLPMO9A and TtPMO1 (PDB-id: 3eii), which scored the highest in a Blast search using the MtLPMO9A sequence against the Protein Data Bank (75% amino acid identity).