Topology of the Ccl1 and HelBCD proteins from System I and the CcsA protein of System II
Topology of proteins involved in heme delivery for cytochrome c biogenesis in Gram-negative bacteria and plant mitochondria. The indicated sequences are from Rhodobacter capsulatus proteins. For the HelC and Ccl1 proteins,
the conserved tryptophan-rich region (called the WWD domain) is periplasmic and is flanked by histidinyl residues (large arrows). As described in Goldman et al, Proc. Natl. Acad. Sci. USA, 1998. 95:5003-5008
Topology of the HelB, HelC, and HelD proteins
The topology of the integral membrane proteins of the HelABCD transporter were determined by the analysis of PhoA fusion proteins which were created at each hydrophilic domain (shown by small arrows). Conserved residues within the bacterial proteins are
from Escherichia coli, Haemophilus influenzae, Paracoccus denitrificans, Pseudomonas fluorescens, Bradyrhizobium japonicum. For conserved residues between the HelC proteins of bacteria and plant mitochondria the above o
rganisms and Oenothera, Dauca, and Marchantia were used. For conserved residues between the HelB proteins of bacteria and plant mitochondria compared the above organisms and Marchantia were used. The heme iron is coordinated to the His1 and His2 residue
s of the HelC protein. The 52 residue HelD polypeptide was previously shown to have its C-terminus in the cytoplasm.
Topology of the Ccl1 protein
The topology of the integral membrane heme protein Ccl1 was determined by analysis of PhoA fusion proteins (Table 1b) which were created at each hydrophilic domain (shown by small arrows). Conserved residues of Ccl1 between bacteria compared the proteins
from Rhodobacter capsulatus, Escherichia coli, Haemophilus influenzae, Paracoccus denitrificans, Rhizobium meliloti, and Bradyrhizobium japonicum. Residues from 1 to 350 of the bacterial Ccl1 protein that are al
so conserved with the plant mitochondria ORF577 of Oenothera, Dauca, and Marchantia. Residues from 351 to 651 are from ORF454 of Oenothera, Brassica, and Arabadopsis.
Topology of the CcsA protein of M. lepraefrom System II
The topology of the CcsA protein of Mycobacterium leprae. Residues of the CcsA protein from M. leprae, M. tuberculosis, and Bacillus subtilis are compared. Topology was determined by the analysis of PhoA fusion proteins which
were created at each of the hydrophilic domains (shown by small arrows). The conserved WWD domain is external and is flanked by histidinyl residues (large arrows). For conserved residues between the CcsA protein of bacteria and chloroplasts, the above
organisms and Chlamydomonas, Porphyra, and Marchantia were used.