4GQW

Crystal structure of CBS-pair protein, CBSX1 (loop deletion) from Arabidopsis thaliana

Summary for 4GQW

• Entry DOI: 10.2210/pdb4gqw/pdb
• Related: 4GQV
• Descriptor: CBS domain-containing protein CBSX1, chloroplastic (2 entities in total)
• Functional Keywords: cbs domain, thioredoxin, chloroplast, plant, protein binding
• Biological source: Arabidopsis thaliana (mouse-ear cress, thale-cress)
• Cellular location: Plastid, chloroplast: O23193
• Total number of polymer chains: 1
• Total formula weight: 16690.12

Authors

Jeong, B.-C.,Song, H.K. (deposition date: 2012-08-24, release date: 2013-01-16, Last modification date: 2024-03-20)

Primary citation

Jeong, B.C.,Park, S.H.,Yoo, K.S.,Shin, J.S.,Song, H.K.
Crystal structure of CBSX1 (loop deletion)
Biochem.Biophys.Res.Commun., 2012

PubMed Abstract: The single cystathionine β-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 β-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 (Δloop) form are reported at resolutions of 2.4 and 2.2Å, respectively. The structures of CBSX1 show that they form anti-parallel dimers along their central twofold axis and have a unique ∼155° 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.

PubMed: 23159611
DOI: 10.1016/j.bbrc.2012.10.139

Experimental method

X-RAY DIFFRACTION (2.201 Å)