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Structure of cytochrome b 5 unique to tardigrades
Author(s) -
Fukuda Yohta,
Kim JeeEun,
Inoue Tsuyoshi
Publication year - 2020
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3896
Subject(s) - cytochrome b , cytochrome , cytochrome c , chemistry , biology , biochemistry , mitochondrion , enzyme , phylogenetic tree , gene
Abstract Cytochrome b 5 is an essential electron transfer protein, which is ubiquitously found in living systems and involved in wide variety of biological processes. Tardigrades (also known as water bears), some of which are famous for desiccation resistance, have many proteins unique to them. Here, we report spectroscopic and structural characterization of a cytochrome b 5 like protein from one of the desiccation‐tolerant tardigrades, Ramazzottius varieornatus strain YOKOZUNA‐1 ( Rv Cyt b 5 ). A 1.4 Å resolution crystal structure revealed that Rv Cyt b 5 is a new cytochrome b 5 protein specific to tardigrades.