6SNR
Crystal structure of FemX
Summary for 6SNR
| Entry DOI | 10.2210/pdb6snr/pdb |
| Descriptor | Lipid II:glycine glycyltransferase (2 entities in total) |
| Functional Keywords | antibiotics, factors essential for meticillin resistance proteins (fem proteins), fem ligases, staphylococcus aureus, femx, enzymes involved in cross-bridge formation, antimicrobial protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 48487.20 |
| Authors | Fulop, V.,Hinxman, K. (deposition date: 2019-08-27, release date: 2020-09-09, Last modification date: 2024-06-19) |
| Primary citation | York, A.,Lloyd, A.J.,Del Genio, C.I.,Shearer, J.,Hinxman, K.J.,Fritz, K.,Fulop, V.,Dowson, C.G.,Khalid, S.,Roper, D.I. Structure-based modeling and dynamics of MurM, a Streptococcus pneumoniae penicillin resistance determinant present at the cytoplasmic membrane. Structure, 29:731-742.e6, 2021 Cited by PubMed Abstract: Branched Lipid II, required for the formation of indirectly crosslinked peptidoglycan, is generated by MurM, a protein essential for high-level penicillin resistance in the human pathogen Streptococcus pneumoniae. We have solved the X-ray crystal structure of Staphylococcus aureus FemX, an isofunctional homolog, and have used this as a template to generate a MurM homology model. Using this model, we perform molecular docking and molecular dynamics to examine the interaction of MurM with the phospholipid bilayer and the membrane-embedded Lipid II substrate. Our model suggests that MurM is associated with the major membrane phospholipid cardiolipin, and experimental evidence confirms that the activity of MurM is enhanced by this phospholipid and inhibited by its direct precursor phosphatidylglycerol. The spatial association of pneumococcal membrane phospholipids and their impact on MurM activity may therefore be critical to the final architecture of peptidoglycan and the expression of clinically relevant penicillin resistance in this pathogen. PubMed: 33740396DOI: 10.1016/j.str.2021.03.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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