Structural highlights
Publication Abstract from PubMed
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 (Deltaloop) form are reported at resolutions of 2.4 and 2.2A, respectively. The structures of CBSX1 show that they form anti-parallel dimers along their central twofold axis and have a unique approximately 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.
Crystal structure of the single cystathionine beta-synthase domain-containing protein CBSX1 from Arabidopsis thaliana.,Jeong BC, Park SH, Yoo KS, Shin JS, Song HK Biochem Biophys Res Commun. 2013 Jan 4;430(1):265-71. doi:, 10.1016/j.bbrc.2012.10.139. Epub 2012 Nov 14. PMID:23159611[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jeong BC, Park SH, Yoo KS, Shin JS, Song HK. Crystal structure of the single cystathionine beta-synthase domain-containing protein CBSX1 from Arabidopsis thaliana. Biochem Biophys Res Commun. 2013 Jan 4;430(1):265-71. doi:, 10.1016/j.bbrc.2012.10.139. Epub 2012 Nov 14. PMID:23159611 doi:http://dx.doi.org/10.1016/j.bbrc.2012.10.139
