Origins of Life and Evolution of Biospheres

, Volume 35, Issue 1, pp 19–27 | Cite as

Sites for Phosphates and Iron-Sulfur Thiolates in the First Membranes: 3 to 6 Residue Anion-Binding Motifs (Nests)

  • E. James Milner-WhiteEmail author
  • Michael J. Russell


Nests are common three to six amino acid residue motifs in proteins where successive main chain NH groups bind anionic atoms or groups. On average 8% of residues in proteins belong to nests. Nests form a key part of a number of phosphate binding sites, notably the P-loop, which is the commonest of the binding sites for the phosphates of ATP and GTP. They also occur regularly in sites that bind [Fe2S2](RS)4 [Fe3S4](RS)3 and [Fe4S4](RS)4 iron-sulfur centers, which are also anionic groups. Both phosphates and iron-sulfur complexes would have occurred in the precipitates within hydrothermal vents of moderate temperature as key components of the earliest metabolism and it is likely existing organisms emerging in this milieu would have benefited from evolving molecules binding such anions. The nest conformation is favored by high proportions of glycine residues and there is evidence for glycine being the commonest amino acid during the stage of evolution when proteins were evolving so it is likely nests would have been common features in peptides occupying the membranes at the dawn of life.


anion hydrothermal inorganic membrane iron-sulfur proteins origin of life pre-biotic phosphate protonmotive force RNA world thiolates 


ϕ, ψ:

For amino acid i, phi (ϕ) is the dihedral angle between the Ci−1-Ni-Cαi-Ci atoms and psi (ψ) is the dihedral angle between the Ni-Cαi-Ci-Ni+1 atoms (i-1 and i+1 are the preceding and succeeding residues).


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© Springer Science + Business Media, Inc. 2005

Authors and Affiliations

  1. 1.Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life SciencesUniversity of GlasgowGlasgowScotland
  2. 2.Scottish Universities Environmental Research CentreGlasgowScotland

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