Identification of potential ferric binding residues in the iron-binding protein of pathogenic Neisseria meningitidis through structure-based multiple sequence alignments.
The ferric iron-binding proteins of pathogenic Neisseria display structural and metal-binding properties characteristic of the transferrin family. In the absence of structural data for the ferric iron-binding proteins, spacial folding templates have been derived for the meningococcal protein from complete and partial structure-based multiple sequence alignments with structurally related proteins. The templates have been used to identify a number of potential iron-binding residues. These include four residues that are identical with the iron coordinating ligands of transferrin, but only two reside within equivalent structural elements.
Gorinsky
B
B
Department of Crystallography, Birkbeck College, London, UK. b.gorinsky@iona.cryst.bbk.ac.uk
Evans
R W
RW
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry*; D005290:Ferric Compounds; D033862:Iron-Binding Proteins; D007781:Lactoferrin / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry*; D033902:Periplasmic Binding Proteins; D017433:Protein Structure, Secondary; D016415:Sequence Alignment / Q000379:methods*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D005290:Ferric Compounds; D033862:Iron-Binding Proteins; D008024:Ligands; D033902:Periplasmic Binding Proteins; D007781:Lactoferrin