1EQ7
CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION
Summary for 1EQ7
| Entry DOI | 10.2210/pdb1eq7/pdb |
| Descriptor | OUTER MEMBRANE LIPOPROTEIN (2 entities in total) |
| Functional Keywords | lipoprotein, outer membrane, protein folding, helix capping, membrane protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 6161.72 |
| Authors | |
| Primary citation | Shu, W.,Liu, J.,Ji, H.,Lu, M. Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. J.Mol.Biol., 299:1101-1112, 2000 Cited by PubMed Abstract: The outer membrane lipoprotein of the Escherichia coli cell envelope has characteristic lipid modifications at an amino-terminal cysteine and can exist in a form bound covalently to the peptidoglycan through a carboxyl-terminal lysine. The 56-residue polypeptide moiety of the lipoprotein, designated Lpp-56, folds into a stable, trimeric helical structure in aqueous solution. The 1.9 A resolution crystal structure of Lpp-56 comprises a parallel three-stranded coiled coil including a novel alanine-zipper unit and two helix-capping motifs. The amino-terminal motif forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The carboxyl-terminal motif uses puckering of the tyrosine side-chains as a unique docking arrangement in helix termination. The structure provides an explanation for assembly and insertion of the lipoprotein molecules into the outer membrane of gram-negative bacteria and suggests a molecular target for antibacterial drug discovery. PubMed: 10843861DOI: 10.1006/jmbi.2000.3776 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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