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Structural characterisation of a MAPR-related archaeal cytochrome b5M protein

  • Sarah Teakel
  • , Michealla Marama
  • , David Aragão
  • , Sofiya Tsimbalyuk
  • , Emily R.R. Mackie
  • , Tatiana P. Soares da Costa
  • , Jade K. Forwood
  • , Michael A. Cahill
  • Australian Synchrotron
  • Diamond Light Source
  • La Trobe University
  • University of Adelaide
  • Australian National University

Research output: Contribution to journalArticlepeer-review

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Abstract

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 b5 (cytb5) domain proteins, called cytb5M (MAPR-like). Relative to classical cytb5 proteins, MAPR and ctyb5M proteins shared unique sequence elements and a distinct heme-binding orientation at an approximately 90° rotation relative to classical cytb5, as demonstrated in the archetypal crystal structure of a cytb5M protein (PDB accession number 6NZX). Here, we present the crystal structure of an archaeal cytb5M domain (Methanococcoides burtonii WP_011499504.1, PDB:6VZ6). It exhibits similar heme binding to the 6NZX cytb5M, supporting the deduction that MAPR-like heme orientation was inherited from the prokaryotic ancestor of the original eukaryotic MAPR gene.
Original languageEnglish
Pages (from-to)2409-2417
Number of pages9
JournalFEBS Letters
Volume596
Issue number18
Early online date09 Aug 2022
DOIs
Publication statusPublished - Sept 2022

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