Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 430, Issue 1, Pages 265-271Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.10.139
Keywords
Arabidopsis thaliana; CBSX1; CBSX2; Cystathionine beta-synthase domain; Plant; Thioredoxin
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Funding
- National Research Foundation of Korea (NRF) grant
- Korean Government (MEST) [2011-0028168]
- Korea Healthcare Technology RAMP
- D Project, Ministry for Health, Welfare AMP
- Family Affairs, Republic of Korea [A092006]
- National Research Foundation of Korea [2011-0028168] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The single cystathionine beta-synthase (CBS) pair proteins from Arabidopsis thaliana have been identified as being a redox regulator of the thioredoxin (Trx) system. CBSX1 and CBSX2, which are two of the six Arabidopsis cystathione beta-synthase domain-containing proteins that contain only a single CBS pair, have close sequence similarity. Recently, the crystal structure of CBSX2 was determined and a significant portion of the internal region was disordered. In this study, crystal structures of full-length CBSX1 and the internal loop deleted (Delta loop) form are reported at resolutions of 2.4 and 2.2 angstrom, respectively. The structures of CBSX1 show that they form anti-parallel dimers along their central twofold axis and have a unique similar to 155 degrees bend along the side. This is different from the angle of CBSX2, which is suggestive of the flexible nature of the relative angle between the monomers. The biochemical data that were obtained using the deletion as well as point mutants of CBSX1 confirmed the importance of AMP-ligand binding in terms of enhancing Trx activity. (C) 2012 Elsevier Inc. All rights reserved.
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