Structural characterisation of a MAPR-related archaeal cytochrome b 5M protein

FEBS Letters

article

Sarah Teakel¹  Michealla Marama²  David Aragão³  Sofiya Tsimbalyuk¹  Emily R. R. Mackie⁴  Tatiana P. Soares da Costa⁴  Jade K. Forwood¹  Michael A. Cahill¹ 

[1] School of Dentistry and Medical Sciences, Charles Sturt University;School of Animal and Veterinary Sciences, Charles Sturt University;Australian Synchrotron, Australian Nuclear Science and Technology Organisation;Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University;School of Agriculture, Food & Wine and Waite Research Institute, University of Adelaide;The John Curtin School of Medical Research, The Australian National University

关键词: cytochrome b5;    membrane-associated progesterone receptor;    steroidogenesis;   

DOI  :  10.1002/1873-3468.14471

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 5 (cytb 5 ) domain proteins, called cytb 5 M ( M APR-like). Relative to classical cytb 5 proteins, MAPR and ctyb 5M proteins shared unique sequence elements and a distinct heme-binding orientation at an approximately 90° rotation relative to classical cytb 5 , 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.

【 授权许可】

Unknown