Premium
Identification of potential ferric binding residues in the iron‐binding protein of pathogenic Neisseria meningitidis through structure‐based multiple sequence alignments
Author(s) -
Gorinsky Beatrice,
Evans Robert W.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00929-0
Subject(s) - transferrin , neisseria meningitidis , neisseria , chemistry , sequence (biology) , peptide sequence , ferric , iron binding proteins , binding site , biochemistry , protein structure , ferric iron , plasma protein binding , sequence alignment , biology , genetics , gene , bacteria , ferrous , organic chemistry
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.