2LAF
NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC
Summary for 2LAF
| Entry DOI | 10.2210/pdb2laf/pdb |
| Related | 2LAE |
| Descriptor | Lipoprotein 34 (1 entity in total) |
| Functional Keywords | beta-barrel assembly machinery, bam, bamc, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane ; Lipid-anchor : P0A903 |
| Total number of polymer chains | 1 |
| Total formula weight | 26998.98 |
| Authors | Pardi, A.,Warner, L. (deposition date: 2011-03-11, release date: 2011-06-01, Last modification date: 2024-05-01) |
| Primary citation | Warner, L.R.,Varga, K.,Lange, O.F.,Baker, S.L.,Baker, D.,Sousa, M.C.,Pardi, A. Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set. J.Mol.Biol., 411:83-95, 2011 Cited by PubMed Abstract: The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein β-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC₁₀₁₋₃₄₄ forms two well-defined domains connected by an ~18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. ¹⁵N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations. PubMed: 21624375DOI: 10.1016/j.jmb.2011.05.022 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
