Identification of potential ferric binding residues in the iron‐binding protein of pathogenic Neisseria meningitidis through structure‐based multiple sequence alignments

FEBS Letters

Evans, Robert W.²  Gorinsky, Beatrice¹ 

[1]Department of Crystallography, Birkbeck College, Malet Street, London WC1 7HX, UK

[2]Division of Biochemistry and Molecular Biology, UMDS, Guy's Hospital, London SE1 9RT, UK

关键词: Ferric iron-binding protein;    Neisseria meningitidis;    Transferrin;    Periplasmic binding protein;    Structure prediction;    Multiple sequence alignment;   

DOI  :  10.1016/S0014-5793(97)00929-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown