Literature DB >> 21798352

Crystal structure of the TL29 protein from Arabidopsis thaliana: an APX homolog without peroxidase activity.

Erik Lundberg1, Patrik Storm, Wolfgang P Schröder, Christiane Funk.   

Abstract

TL29 is a plant-specific protein found in the thylakoid lumen of chloroplasts. Despite the putative requirement in plants for a peroxidase close to the site of photosynthetic oxygen production, and the sequence homology of TL29 to ascorbate peroxidases, so far biochemical methods have not shown this enzyme to possess peroxidase activity. Here we report the three-dimensional X-ray crystal structure of recombinant TL29 from Arabidopsis thaliana at a resolution of 2.5Å. The overall structure of TL29 is mainly alpha helical with six longer and six shorter helical segments. The TL29 structure resembles that of typical ascorbate peroxidases, however, crucial differences were found in regions that would be important for heme and ascorbate binding. Such differences suggest it to be highly unlikely that TL29 functions as a peroxidase.
Copyright © 2011 Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21798352     DOI: 10.1016/j.jsb.2011.07.004

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  3 in total

1.  The APX4 locus regulates seed vigor and seedling growth in Arabidopsis thaliana.

Authors:  Ya-Ying Wang; Amanda G Hecker; Bernard A Hauser
Journal:  Planta       Date:  2014-01-10       Impact factor: 4.116

Review 2.  Understanding the roles of the thylakoid lumen in photosynthesis regulation.

Authors:  Sari Järvi; Peter J Gollan; Eva-Mari Aro
Journal:  Front Plant Sci       Date:  2013-10-31       Impact factor: 5.753

3.  Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida.

Authors:  Fernanda Lazzarotto; Paloma Koprovski Menguer; Luiz-Eduardo Del-Bem; Marcel Zámocký; Márcia Margis-Pinheiro
Journal:  Antioxidants (Basel)       Date:  2021-04-13
  3 in total

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