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. 2008 Sep 12;59(14):3885–3901. doi: 10.1093/jxb/ern226

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© 2008 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 4. — Schematic representation of the three-dimensional structures of monomers of (A) Xhdsi-1^VOC (B), human glyoxalase I (1FRO.pdb) (C) Atdsi-1^VOC (D) Leishmania major glyoxalase I protein (2C21.pdb) (E) unknown Arabidopsis protein encoded by At5g48480 (1XY7.pdb), and (F) Klebsiella pneumoniae bleomycin resistance protein (1ECS.pdb). The tertiary structure of Xhdsi-1^VOC was predicted using the A chain of human glyoxalase I (B) as a template, while the tertiary structure of Atdsi-1^VOC was predicted using the A chain of bacterial glyoxalase I (D) as a template, via the EsyPred3D server. The unknown Arabidopsis protein (E) and bleomycin resistant protein (F) were selected as the closest structural matches to Xhdsi-1^VOC by mGenThreader. The monomers have been colour ramped according to residue number, starting with blue (N-terminus) and finishing with red (C-terminus). The first βαβββ repeat of the human glyoxalase I protein is numbered in (B), while the predicted α-helices and β-sheets for Xhdsi-1^VOC and Atdsi-1^VOC are annotated in (A) and (C), respectively.