7ZOT
crystal structure of PLAAT4 N-terminal domain
Summary for 7ZOT
| Entry DOI | 10.2210/pdb7zot/pdb |
| Descriptor | Phospholipase A and acyltransferase 4, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | phospholipase a1/a2, acyltransferase, catalytic domain, soluble domain, cytosolic protein, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 28197.81 |
| Authors | von Castelmur, E.,Perrakis, A.,Cornaciu, I. (deposition date: 2022-04-26, release date: 2022-10-26, Last modification date: 2024-01-31) |
| Primary citation | Wehlin, A.,Cornaciu, I.,Marquez, J.A.,Perrakis, A.,von Castelmur, E. Crystal structure of the phospholipase A and acyltransferase 4 (PLAAT4) catalytic domain. J.Struct.Biol., 214:107903-107903, 2022 Cited by PubMed Abstract: Phospholipase A and Acyltransferase 4 (PLAAT4) is a class II tumor suppressor, that also plays a role as a restrictor of intracellular Toxoplasma gondii infection through restriction of parasitic vacuole size. The catalytic N-terminal domain (NTD) interacts with the C-terminal domain (CTD), which is important for sub-cellular targeting and enzymatic function. The dynamics of the NTD main (L1) loop and the L2(B6) loop adjacent to the active site, have been shown to be important regulators of enzymatic activity. Here, we present the crystal structure of PLAAT4 NTD, determined from severely intergrown crystals using automated, laser-based crystal harvesting and data reduction technologies. The structure showed the L1 loop in two distinct conformations, highlighting a complex network of interactions likely influencing its conformational flexibility. Ensemble refinement of the crystal structure recapitulates the major correlated motions observed in solution by NMR. Our analysis offers useful insights on millisecond dynamics based on the crystal structure, complementing NMR studies which preclude structural information at this time scale. PubMed: 36210037DOI: 10.1016/j.jsb.2022.107903 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.735 Å) |
Structure validation
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