Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction.
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.
Dunten
P
P
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
Mowbray
S L
SL
D001426:Bacterial Proteins; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004926:Escherichia coli / Q000737:chemistry; D006193:Haemophilus influenzae / Q000737:chemistry*; D006418:Heme / Q000378:metabolism*; D008074:Lipoproteins / Q000737:chemistry* / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry; D008958:Models, Molecular; D017385:Sequence Homology; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D002352:Carrier Proteins; C097952:HbpA protein, Haemophilus influenzae; D008074:Lipoproteins; D026901:Membrane Transport Proteins; C037230:oligopeptide permease, Bacteria; D006418:Heme