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Among all the proteins of Periplasmic C type cytochrome A (PPCA) familyobtained from cytochrome C7 found in Geobacter sulfurreducens, PPCA protein caninteract with Deoxycholate (DXCA), while its other homologs do not, as observedfrom the crystal structures. Utilizing the concept of 'structure-functionrelationship', an effort has been initiated towards understanding the drivingforce for recognition of DXCA exclusively by PPCA among its homologs. Further,a combinatorial analysis of the binding sequences (contiguous sequence of aminoacid residues of binding locations) is performed to build graph-theoreticmodels, which show that PPCA differs from its homologues. Analysis of theresults suggests that the underlying impetus of recognition of DXCA by PPCA isembedded in its primary sequence and 3D conformation.

Understanding the behavioural difference of PPCA among its homologs in C7 family towards recognition of DXCA