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Article Dans Une Revue Metallomics Année : 2012

Identification of two-histidines one-carboxylate binding motifs in proteins amenable to facial coordination to metals.

Résumé

Among natural metalloenzymes, the facial two-histidines one-carboxylate binding motif (FTM) is a widely represented first coordination sphere motif present in the active site of a variety of metalloenzymes. A PDB search revealed a total of 1685 structures bearing such FTMs bound to a metal. Sixty statistically representative FTMs were selected and used as template for the identification of structurally characterized proteins bearing these three amino acids in a propitious environment for binding to a transition metal. This geometrical superposition search, carried out using the STAMPS software, returned 2320 hits. While most consisted of either apo-FTMs or bore strong sequence homology to known FTMs, seven such structures lying within a cavity were identified as novel and viable scaffolds for the creation of artificial metalloenzymes bearing an FTM.

Dates et versions

hal-00738089 , version 1 (03-10-2012)

Identifiants

Citer

Beat Amrein, Maurus Schmid, Guillaume Collet, Philippe Cuniasse, François Gilardoni, et al.. Identification of two-histidines one-carboxylate binding motifs in proteins amenable to facial coordination to metals.. Metallomics, 2012, 4 (4), pp.379-88. ⟨10.1039/c2mt20010d⟩. ⟨hal-00738089⟩
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