3PTJ
Structural and functional Analysis of Arabidopsis thaliana thylakoid lumen protein AtTLP18.3
Summary for 3PTJ
| Entry DOI | 10.2210/pdb3ptj/pdb |
| Related | 3PVH 3PW9 |
| Descriptor | UPF0603 protein At1g54780, chloroplastic (2 entities in total) |
| Functional Keywords | tap domain, rossmann fold, acid phosphatase, arabidopsis thaliana thylakoid lumen, hydrolase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Plastid, chloroplast thylakoid membrane ; Single-pass membrane protein ; Lumenal side : Q9ZVL6 |
| Total number of polymer chains | 1 |
| Total formula weight | 16779.55 |
| Authors | Wu, H.Y.,Liu, M.S.,Lin, T.P.,Cheng, Y.S. (deposition date: 2010-12-03, release date: 2011-10-26, Last modification date: 2024-10-16) |
| Primary citation | Wu, H.Y.,Liu, M.S.,Lin, T.P.,Cheng, Y.S. Structural and functional assays of AtTLP18.3 identify its novel acid phosphatase activity in thylakoid lumen Plant Physiol., 157:1015-1025, 2011 Cited by PubMed Abstract: The membrane protein AtTLP18.3 of Arabidopsis (Arabidopsis thaliana) contains a domain of unknown function, DUF477; it forms a polysome with photosynthetic apparatuses in the thylakoid lumen. To explore the molecular function of AtTLP18.3, we resolved its crystal structures with residues 83 to 260, the DUF477 only, and performed a series of biochemical analyses to discover its function. The gene expression of AtTLP18.3 followed a circadian rhythm. X-ray crystallography revealed the folding of AtTLP18.3 as a three-layer sandwich with three α-helices in the upper layer, four β-sheets in the middle layer, and two α-helices in the lower layer, which resembles a Rossmann fold. Structural comparison suggested that AtTLP18.3 might be a phosphatase. The enzymatic activity of AtTLP18.3 was further confirmed by phosphatase assay with various substrates (e.g. p-nitrophenyl phosphate, 6,8-difluoro-4-methylumbelliferyl phosphate, O-phospho-L-serine, and several synthetic phosphopeptides). Furthermore, we obtained the structure of AtTLP18.3 in complex with O-phospho-L-serine to identify the binding site of AtTLP18.3. Our structural and biochemical studies revealed that AtTLP18.3 has the molecular function of a novel acid phosphatase in the thylakoid lumen. DUF477 is accordingly renamed the thylakoid acid phosphatase domain. PubMed: 21908686DOI: 10.1104/pp.111.184739 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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