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Fig. 6 | BMC Biochemistry

Fig. 6

From: Purification and characterization of a cytochrome c with novel caspase-3 activation activity from the pathogenic fungus Rhizopus arrhizus

Fig. 6

a Sequence alignment of R. arrhizus cyt c with human, horse, and budding yeast cyt c. The shaded areas are the residues (in horse) essentially involved in Apaf-1 binding. Residues in R. arrhizus showing charge reversal/neutralization (with respect to horse Lys) substitutions are shown in green. The numbering position of residues is with respect to horse cyt c. b Protein models of R. arrhizus and horse cyt c showing positions of 3 important lysine residues involved in Apaf-1 binding. From left to right: R. arrhizus model (generated using Swiss-model homology modeling server) and horse cyt c (PDB ID-1HRC). In R. arrhizus, two residues important for Apaf-1 binding, lysine 7 and 25 (red) are substituted by alanine. Another important lysine residue (blue) is conserved in both R. arrhizus and horse cyt c. Both images were generated using PyMOL

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BMC Biochemistry

ISSN: 1471-2091

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