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. 2014 Jan 22;7:11. doi: 10.1186/1754-6834-7-11

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Copyright © 2014 Biswal et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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 features of PtxtPL1-27. (A) Structure of mRNA [GenBank: EU379971.1]. Cds, coding sequence; nt, nucleotides. (B) Structure of the deduced peptide showing the signal peptide (SP), the pectate lyase C catalytic domain, and the predicted N-glycosylation site (N). AA, amino acids. (C) A multiple alignment of the catalytic site of PtxtPL1-27 and pectate lyases of known enzymatic activities, showing the conserved residues involved in Ca⁺² binding (pink), disulfide bonds (orange), catalysis (blue), and substrate binding (gray) with numbering according to Pel C structure as in [16]. ZePel, Zinnia elegans pectate lyase; MaPel1, Musa acuminata pectate lyase 1; Pel C, Erwinia chrysanthemi pectate lyase C.