Structural characterisation of a MAPR-related archaeal cytochrome b protein.

We recently reported that the membrane-associated progesterone receptor (MAPR) protein family (mammalian members: PGRMC1, PGRMC2, NEUFC and NENF) originated from a new class of prokaryotic cytochrome b (cytb ) domain proteins, called cytb (MAPR-like). Relative to classical cytb proteins, MAPR and ctyb proteins shared unique sequence elements and a distinct heme-binding orientation at an approximately 90° rotation relative to classical cytb , as demonstrated in the archetypal crystal structure of a cytb protein (PDB accession number 6NZX). Here, we present the crystal structure of an archaeal cytb domain (Methanococcoides burtonii WP_011499504.1, PDB:6VZ6). It exhibits similar heme binding to the 6NZX cytb , supporting the deduction that MAPR-like heme orientation was inherited from the prokaryotic ancestor of the original eukaryotic MAPR gene.