Protein Family Models

Iteration of the HHE family ([2]) found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain ([1]) in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor Swiss:P80255 binds Cadmium so as to protect the organism from toxicity ([3]). However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial Swiss:Q7WX96 is a regulator of response to NO, which suggests yet another set-up for its metal ligands ([4]). In Staphylococcus aureus P72360 has been noted to be important when the organism switches to living in environments with low oxygen concentrations ([4]); perhaps this protein acts as an oxygen store or scavenger. This domain can bind oxygen (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043) [1]. 678527. Structure of methemerythrin at 2.8-Angstrom resolution: computer graphics fit of an averaged electron density map. Stenkamp RE, Sieker LC, Jensen LH, McQueen JE Jr;. Biochemistry 1978;17:2499-2504. [2]. 12625841. New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3. [3]. 9188702. Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution. Martins LJ, Hill CP, Ellis WR Jr;. Biochemistry 1997;36:7044-7049. [4]. 11513618. The srhSR gene pair from Staphylococcus aureus: genomic and proteomic approaches to the . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

hemerythrin domain-containing protein adopts a four alpha helix bundle fold and may bind cations

Date:

2017-12-04