1EQ7

CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION

1EQ7 の概要

• エントリーDOI: 10.2210/pdb1eq7/pdb
• 分子名称: OUTER MEMBRANE LIPOPROTEIN (2 entities in total)
• 機能のキーワード: lipoprotein, outer membrane, protein folding, helix capping, membrane protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6161.72

構造登録者

Shu, W.,Liu, J.,Ji, H.,Lu, M. (登録日: 2000-04-03, 公開日: 2000-06-28, 最終更新日: 2024-02-07)

主引用文献

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

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: 10843861
DOI: 10.1006/jmbi.2000.3776

実験手法

X-RAY DIFFRACTION (1.9 Å)