6LKB
Crystal Structure of the peptidylprolyl isomerase domain of Arabidopsis thaliana CYP71.
Summary for 6LKB
| Entry DOI | 10.2210/pdb6lkb/pdb |
| Descriptor | Peptidyl-prolyl cis-trans isomerase CYP71, GLYCEROL, COBALT (II) ION, ... (6 entities in total) |
| Functional Keywords | ppiase, cyp71, cyclophilin, chromatin remodelling, isomerase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 36853.76 |
| Authors | Lakhanpal, S.,Jobichen, C.,Swaminathan, K. (deposition date: 2019-12-18, release date: 2020-12-16, Last modification date: 2023-11-22) |
| Primary citation | Lakhanpal, S.,Fan, J.S.,Luan, S.,Swaminathan, K. Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3. Febs Lett., 595:145-154, 2021 Cited by PubMed Abstract: Arabidopsis thaliana CYP71 (AtCYP71) is a chromatin-remodeling protein that promotes shoot apical meristem (SAM) differentiation. The N terminus of AtCYP71 contains a noncanonical WD domain, and the C terminus contains an enzymatic peptidyl-prolyl isomerase (PPIase) cyclophilin (CYP) domain. To date, there has been no characterization of CYP71, and its mode of action remains unknown. Here, we report the crystal structure of the CYP domain of AtCYP71 at 1.9 Å resolution. The structure shows key differences when compared to the canonical CYP fold of human CypA. To the best our knowledge, this is the first A. thaliana CYP structure with a conserved active site loop. Using nuclear magnetic resonance spectroscopy, we demonstrate that the CYP domain is active toward histone H3. Our findings suggest that the PPIase activity of the CYP domain is important for the function of AtCYP71 in chromatin remodeling during organogenesis. PubMed: 33098102DOI: 10.1002/1873-3468.13965 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.651 Å) |
Structure validation
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