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Protein Sci. 1995 Nov;4(11):2335-40.

Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction.

Author information

1
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.

Abstract

The structure and function of the periplasmic heme-binding protein HbpA of Haemophilus influenzae were investigated. This protein is involved in the import of heme into the bacteria through the inner membrane, and thus is a key element of the organism's ability to survive in blood. A high degree of sequence similarity between HbpA and the dipeptide-binding protein of Escherichia coli is suggested to be the result of a functional relationship. An HbpA model built using the dipeptide-binding protein suggests a mode of heme binding that is distinct from those known in proteins of the human host. These results provide a starting point for rational drug design.

PMID:
8563630
PMCID:
PMC2143024
DOI:
10.1002/pro.5560041111
[Indexed for MEDLINE]
Free PMC Article

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