2KM7
Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli
Summary for 2KM7
| Entry DOI | 10.2210/pdb2km7/pdb |
| Descriptor | Small protein A (1 entity in total) |
| Functional Keywords | bame, smpa, bam complex, omp85, yaet, cell membrane, cell outer membrane, lipoprotein, membrane, palmitate, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Lipid-anchor: P0A937 |
| Total number of polymer chains | 1 |
| Total formula weight | 11446.64 |
| Authors | Knowles, T.J.,Sridhar, P.,Rajesh, S.,Manoli, E.,Henderson, I.R.,Overduin, M. (deposition date: 2009-07-24, release date: 2011-02-02, Last modification date: 2024-05-22) |
| Primary citation | Knowles, T.J.,Browning, D.F.,Jeeves, M.,Maderbocus, R.,Rajesh, S.,Sridhar, P.,Manoli, E.,Emery, D.,Sommer, U.,Spencer, A.,Leyton, D.L.,Squire, D.,Chaudhuri, R.R.,Viant, M.R.,Cunningham, A.F.,Henderson, I.R.,Overduin, M. Structure and function of BamE within the outer membrane and the beta-barrel assembly machine. Embo Rep., 12:123-128, 2011 Cited by PubMed Abstract: Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex. PubMed: 21212804DOI: 10.1038/embor.2010.202 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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