scholarly journals The Effect of Heme Binding on the Tryptophan Residue and the Protein Conformation of Cytochrome b5

1972 ◽  
Vol 247 (14) ◽  
pp. 4641-4647 ◽  
Author(s):  
Thomas E. Huntley ◽  
Philipp Strittmatter
Keyword(s):  
Protein Conformation ◽  
Cytochrome B5 ◽  
Tryptophan Residue ◽  
Heme Binding

scholarly journals Phospholipid membranes affect tertiary structure of the soluble cytochrome b5 heme-binding domain

2008 ◽  
Vol 1778 (4) ◽  
pp. 1015-1026 ◽  
Author(s):  
Liana V. Basova ◽  
Elisaveta I. Tiktopulo ◽  
Victor P. Kutyshenko ◽  
A. Grant Mauk ◽  
Valentina E. Bychkova
Keyword(s):  
Tertiary Structure ◽  
Cytochrome B5 ◽  
Binding Domain ◽  
Phospholipid Membranes ◽  
Heme Binding

scholarly journals MAPR origins reveal a new class of prokaryotic cytochrome b5 proteins and possible role in eukaryogenesis

2021 ◽  
Author(s):  
Daniel Tamarit ◽  
Sarah Teakel ◽  
Michealla Marama ◽  
David Aragão ◽  
Svetlana Y. Gerdes ◽  
...  
Keyword(s):  
Family Member ◽  
Membrane Trafficking ◽  
Cytochrome B5 ◽  
Sterol Metabolism ◽  
Heme Binding ◽  
Eukaryotic Evolution ◽  
Multiple Functions ◽  
New Class ◽  
Steroid Responsiveness ◽  
Candidate Phyla Radiation

The multiple functions of PGRMC1, the archetypal heme-binding eukaryotic MAPR family member, include steroidogenic regulation, membrane trafficking, and steroid responsiveness. The interrelationships between these functions are currently poorly understood. Previous work has shown that different MAPR subclasses were present early in eukaryotic evolution, and that tyrosine phosphorylated residues appeared in the eumetazoan ancestor, coincident with a gastrulation organizer. Here we show that MAPR proteins are related to a newly recognized class of prokaryotic cytochrome-b5 domain proteins. Our first solved structure of this new class exhibits shared MAPR-like folded architecture and heme-binding orientation. We also report that a protein subgroup from Candidate Phyla Radiation (CPR) bacteria shares MAPR-like heme-interacting tyrosines. Our results support bacterial origins for both PGRMC1 and CYP51A, that catalyze the meiosis-associated 14-demethylation of the first sterol lanosterol from yeast to humans. We propose that eukaryotic acquisition of a membrane-trafficking function related to sterol metabolism was associated with the appearance of MAPR genes early in eukaryotic evolution.

scholarly journals Amino-acid sequence of the cytochrome-b5-like heme-binding domain from Hansenula anomala flavocytochrome b2

1987 ◽  
Vol 169 (3) ◽  
pp. 539-544 ◽  
Author(s):  
Pierre-Yves HAUMONT ◽  
Marie-Antoinette THOMAS ◽  
Francoise LABEYRIE ◽  
Florence LEDERER
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cytochrome B5 ◽  
Binding Domain ◽  
Heme Binding ◽  
Flavocytochrome B2 ◽  
Hansenula Anomala

scholarly journals Insertion of the cytochrome b5 heme-binding loop into an SH3 domain. Effects on structure and stability, and clues about the cytochrome's architecture

2008 ◽  
Vol 13 (11) ◽  
pp. 2899-2908 ◽  
Author(s):  
Jane A. Knappenberger ◽  
Christina M. Kraemer-Pecore ◽  
Juliette T.J. Lecomte
Keyword(s):  
Cytochrome B5 ◽  
Sh3 Domain ◽  
Heme Binding ◽  
Structure And Stability ◽  
Binding Loop

scholarly journals The distinct heme coordination environments and heme-binding stabilities of His39Ser and His39Cys mutants of cytochrome b5

2003 ◽  
Vol 16 (12) ◽  
pp. 1047-1054 ◽  
Author(s):  
W.-H. Wang ◽  
J.-X. Lu ◽  
P. Yao ◽  
Y. Xie ◽  
Z.-X. Huang
Keyword(s):  
Cytochrome B5 ◽  
Heme Binding

scholarly journals Structural characterization of a MAPR-related archaeal cytochrome b5M protein

2021 ◽  
Author(s):  
Sarah Teakel ◽  
Michealla Marama ◽  
David Aragão ◽  
Sofiya Tsimbalyuk ◽  
Jade K. Forwood ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Progesterone Receptor ◽  
Structural Characterization ◽  
Cytochrome B5 ◽  
Unique Sequence ◽  
Heme Binding ◽  
Accession Number ◽  
New Class ◽  
Sequence Elements

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 90⁰ rotation relative to classical cytb5, as demonstrated in the archetypal crystal structure of a cytb5M protein (PDB accession number 6NZX). Here, we present the second 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.

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