1k24 | pdb_00001k24

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

spinqualitylabelsall models 1k24, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1k24 is a 1 chain structure with sequence from Neisseria meningitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, ZN Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis.,Prince SM, Achtman M, Derrick JP Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3417-21. Epub 2002 Mar 12. PMID:11891340 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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