5EG1
Antibacterial peptide ABC transporter McjD with a resolved lipid
Summary for 5EG1
| Entry DOI | 10.2210/pdb5eg1/pdb |
| Related | 4PL0 |
| Descriptor | Microcin-J25 export ATP-binding/permease protein McjD, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | membrane protein, abc transporter, lipid, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : Q9X2W0 |
| Total number of polymer chains | 2 |
| Total formula weight | 132772.83 |
| Authors | Choudhury, H.G.,Beis, K. (deposition date: 2015-10-26, release date: 2016-08-31, Last modification date: 2024-01-10) |
| Primary citation | Mehmood, S.,Corradi, V.,Choudhury, H.G.,Hussain, R.,Becker, P.,Axford, D.,Zirah, S.,Rebuffat, S.,Tieleman, D.P.,Robinson, C.V.,Beis, K. Structural and Functional Basis for Lipid Synergy on the Activity of the Antibacterial Peptide ABC Transporter McjD. J.Biol.Chem., 291:21656-21668, 2016 Cited by PubMed Abstract: The lipid bilayer is a dynamic environment that consists of a mixture of lipids with different properties that regulate the function of membrane proteins; these lipids are either annular, masking the protein hydrophobic surface, or specific lipids, essential for protein function. In this study, using tandem mass spectrometry, we have identified specific lipids associated with the Escherichia coli ABC transporter McjD, which translocates the antibacterial peptide MccJ25. Using non-denaturing mass spectrometry, we show that McjD in complex with MccJ25 survives the gas phase. Partial delipidation of McjD resulted in reduced ATPase activity and thermostability as shown by circular dichroism, both of which could be restored upon addition of defined E. coli lipids. We have resolved a phosphatidylglycerol lipid associated with McjD at 3.4 Å resolution, whereas molecular dynamic simulations carried out in different lipid environments assessed the binding of specific lipids to McjD. Combined, our data show a synergistic effect of zwitterionic and negatively charged lipids on the activity of McjD; the zwitterionic lipids provide structural stability to McjD, whereas the negatively charged lipids are essential for its function. PubMed: 27555327DOI: 10.1074/jbc.M116.732107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.42 Å) |
Structure validation
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