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

doi:10.1002/1873-3468.14471

Structural characterisation of a MAPR-related archaeal cytochrome b_5M protein

Sarah Teakel
, Michealla Marama
, David Aragão
, Sofiya Tsimbalyuk
, Emily R.R. Mackie
, Tatiana P. Soares da Costa
, Jade K. Forwood^*
, Michael A. Cahill^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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 cytb_5M (MAPR-like). Relative to classical cytb₅ proteins, MAPR and ctyb_5M 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 cytb_5M protein (PDB accession number 6NZX). Here, we present the crystal structure of an archaeal cytb_5M domain (Methanococcoides burtonii WP_011499504.1, PDB:6VZ6). It exhibits similar heme binding to the 6NZX cytb_5M, supporting the deduction that MAPR-like heme orientation was inherited from the prokaryotic ancestor of the original eukaryotic MAPR gene.

Original language	English
Pages (from-to)	2409-2417
Number of pages	9
Journal	FEBS Letters
Volume	596
Issue number	18
DOIs	https://doi.org/10.1002/1873-3468.14471
Publication status	Published - Sept 2022

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@article{8cba6e5a47024dd8bd69f9ba4945a52c,

title = "Structural characterisation of a MAPR-related archaeal cytochrome b5M protein",

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.",

keywords = "cytochrome b5, membrane-associated progesterone receptor, steroidogenesis",

author = "Sarah Teakel and Michealla Marama and David Arag{\~a}o and Sofiya Tsimbalyuk and Mackie, \{Emily R.R.\} and \{Soares da Costa\}, \{Tatiana P.\} and Forwood, \{Jade K.\} and Cahill, \{Michael A.\}",

note = "Publisher Copyright: {\textcopyright} 2022 The Authors. FEBS Letters published by John Wiley \& Sons Ltd on behalf of Federation of European Biochemical Societies.",

year = "2022",

month = sep,

doi = "10.1002/1873-3468.14471",

language = "English",

volume = "596",

pages = "2409--2417",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley \& Sons Inc.",

number = "18",

}

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.

PY - 2022/9

Y1 - 2022/9

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

UR - https://www.scopus.com/pages/publications/85136457573

U2 - 10.1002/1873-3468.14471

DO - 10.1002/1873-3468.14471

M3 - Article

SN - 0014-5793

VL - 596

SP - 2409

EP - 2417

JO - FEBS Letters

JF - FEBS Letters

IS - 18

ER -

Structural characterisation of a MAPR-related archaeal cytochrome b_5M protein

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