5KYM
Crystal Structure of the 1-acyl-sn-glycerophosphate (LPA) acyltransferase, PlsC, from Thermotoga maritima
Summary for 5KYM
| Entry DOI | 10.2210/pdb5kym/pdb |
| Descriptor | 1-acyl-sn-glycerol-3-phosphate acyltransferase, 1-HEPTADECANOYL-2-TRIDECANOYL-3-GLYCEROL-PHOSPHONYL CHOLINE, nonane, ... (5 entities in total) |
| Functional Keywords | integral membrane, membrane helices, hx4d acyltransferase, alpha-beta structure, 1-acyl-sn-glycerol-3-phosphate acyltransferase, transferase |
| Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
| Total number of polymer chains | 2 |
| Total formula weight | 62496.86 |
| Authors | Robertson, R.M.,Yao, J.,Gajewski, S.,Kumar, G.,Martin, E.W.,Rock, C.O.,White, S.W. (deposition date: 2016-07-21, release date: 2017-07-26, Last modification date: 2024-03-06) |
| Primary citation | Robertson, R.M.,Yao, J.,Gajewski, S.,Kumar, G.,Martin, E.W.,Rock, C.O.,White, S.W. A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer. Nat. Struct. Mol. Biol., 24:666-671, 2017 Cited by PubMed Abstract: Phosphatidic acid (PA), the central intermediate in membrane phospholipid synthesis, is generated by two acyltransferases in a pathway conserved in all life forms. The second step in this pathway is catalyzed by 1-acyl-sn-glycerol-3-phosphate acyltransferase, called PlsC in bacteria. Here we present the crystal structure of PlsC from Thermotoga maritima, revealing an unusual hydrophobic/aromatic N-terminal two-helix motif linked to an acyltransferase αβ-domain that contains the catalytic HXD motif. PlsC dictates the acyl chain composition of the 2-position of phospholipids, and the acyl chain selectivity 'ruler' is an appropriately placed and closed hydrophobic tunnel. We confirmed this by site-directed mutagenesis and membrane composition analysis of Escherichia coli cells that expressed mutant PlsC. Molecular dynamics (MD) simulations showed that the two-helix motif represents a novel substructure that firmly anchors the protein to one leaflet of the membrane. This binding mode allows the PlsC active site to acylate lysophospholipids within the membrane bilayer by using soluble acyl donors. PubMed: 28714993DOI: 10.1038/nsmb.3436 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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