4.4 Article

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

期刊

JOURNAL OF STRUCTURAL BIOLOGY
卷 176, 期 1, 页码 24-31

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2011.07.004

关键词

APX4; Thylakoid lumen; Ascorbate peroxidase

资金

  1. Swedish Research Council (VR) [621-2008-3207]
  2. Swedish Energy Agency
  3. Royal Swedish Academy of Sciences
  4. Umea University
  5. Kempe foundation

向作者/读者索取更多资源

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 2.5 angstrom. 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. (C) 2011 Elsevier Inc. All rights reserved.

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