TY - JOUR
T1 - Structural characterisation of a MAPR-related archaeal cytochrome b5M protein
AU - Teakel, Sarah
AU - Marama, Michealla
AU - Aragão, David
AU - Tsimbalyuk, Sofiya
AU - Mackie, Emily R.R.
AU - Soares da Costa, Tatiana P.
AU - Forwood, Jade K.
AU - Cahill, Michael A.
N1 - Funding Information:
This research was supported by Charles Sturt University School of Biomedical Sciences (MAC), an APA PhD scholarship (ST), an Australian Government Research Training Program Scholarship (ERRM) and a Grains Research and Development Corporation (9176977) PhD scholarship (ERRM) and operational funding (JKF, ERRM). This research was partly undertaken on the macromolecular crystallography beamlines at the Australian Synchrotron, part of ANSTO (DA). TPSC would like to thank the Australian Research Council (DE190100806) for fellowship and funding support. We also thank the La Trobe University Comprehensive Proteomics Platform for providing infrastructure support. Open access publishing facilitated by Charles Sturt University, as part of the Wiley ‐ Charles Sturt University agreement via the Council of Australian University Librarians. Open access publishing facilitated by Charles Sturt University, as part of the Wiley ‐ Charles Sturt University agreement via the Council of Australian University Librarians.
Publisher Copyright:
© 2022 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
PY - 2022/8/9
Y1 - 2022/8/9
N2 - 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.
AB - 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.
KW - cytochrome b5
KW - membrane-associated progesterone receptor
KW - steroidogenesis
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U2 - 10.1002/1873-3468.14471
DO - 10.1002/1873-3468.14471
M3 - Article
C2 - 35993565
AN - SCOPUS:85136457573
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
ER -