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Evolution of Staircase Structures in Diffusive Convection

Evolution of Staircase Structures in Diffusive Convection

Published on: September 5, 2018

Structure, function and evolution of the hemerythrin-like domain superfamily.

Claudia Alvarez-Carreño¹, Vikram Alva², Arturo Becerra¹

¹Facultad de Ciencias, Universidad Nacional Autónoma de México, Apdo. Postal 70-407, Cd. Universitaria, Mexico City, 04510, Mexico.

Protein Science : a Publication of the Protein Society

|January 14, 2018

Summary

The hemerythrin-like protein superfamily shows diverse functions beyond oxygen binding. Classification reveals three main groups based on iron-coordinating residues, suggesting a common evolutionary origin.

Keywords:

hemerythrin-like superfamily subgroups nonheme iron protein oxygen-binding protein up-and-down bundle

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Last Updated: Feb 15, 2026

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Published on: September 5, 2018

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Published on: May 29, 2008

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Hemerythrin-like proteins are known for oxygen transport via nonheme iron centers.
Emerging evidence highlights diverse biological roles for this protein superfamily.
Examples include nitric oxide reduction and iron homeostasis.

Purpose of the Study:

To systematically investigate the functional and structural diversity of hemerythrin-like proteins.
To classify hemerythrin-like protein families based on conserved sequence motifs.
To explore the evolutionary origins of the hemerythrin domain.

Main Methods:

Collected hemerythrin-like sequences from a comprehensive proteome database.
Generated a cluster map using all-against-all pairwise sequence similarity.
Classified protein families based on cation-coordinating residues.

Main Results:

Identified a large number of protein families within the hemerythrin-like superfamily.
Classified these families into three main groups based on conserved motifs: signal-transduction/oxygen-carrier, hemerythrin-like, and metazoan F-box proteins.
Observed internal sequence and structural symmetry in most families, suggesting a duplication event origin.

Conclusions:

The hemerythrin-like superfamily is functionally and structurally diverse.
Classification based on cation-coordinating residues provides a framework for understanding this diversity.
A duplication event likely contributed to the evolution of the hemerythrin domain.