1K24

Crystal Structure of the OpcA Outer Membrane Adhesin/Invasin from Neisseria meningitidis

Summary for 1K24

• Entry DOI: 10.2210/pdb1k24/pdb
• Descriptor: outer membrane protein, ZINC ION, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: adhesin, invasin, membrane protein, outer membrane, beta barrel
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 28765.43

Authors

Prince, S.M.,Achtman, M.,Derrick, J.P. (deposition date: 2001-09-26, release date: 2002-03-27, Last modification date: 2024-02-07)

Primary citation

Prince, S.M.,Achtman, M.,Derrick, J.P.
Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis.
Proc.Natl.Acad.Sci.USA, 99:3417-3421, 2002

PubMed Abstract: OpcA is an integral outer membrane protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It mediates the adhesion of N. meningitidis to epithelial and endothelial cells by binding to vitronectin and proteoglycan cell-surface receptors. Here, we report the determination of the crystal structure of OpcA to 2.0 A resolution. OpcA adopts a 10-stranded beta-barrel structure with extensive loop regions that protrude above the predicted surface of the membrane. The second external loop adopts an unusual conformation, traversing the axis of the beta-barrel and apparently blocking formation of a pore through the membrane. Loops 2, 3, 4, and 5 associate to form one side of a crevice in the external surface of the structure, the other side being formed by loop 1. The crevice is lined by positively charged residues and would form an ideal binding site for proteoglycan polysaccharide. The structure, therefore, suggests a model for how adhesion of this important human pathogen to proteoglycan is mediated at the molecular level.

PubMed: 11891340
DOI: 10.1073/pnas.062630899

Experimental method

X-RAY DIFFRACTION (2.03 Å)