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

Metallomics : integrated biometal science (2012-03-07)
Beat Amrein, Maurus Schmid, Guillaume Collet, Philippe Cuniasse, François Gilardoni, Florian P Seebeck, Thomas R Ward
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.

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Carboxypeptidase A from bovine pancreas, (Type II-PMSF treated), ≥50 units/mg protein, ready-to-use solution
Sigma-Aldrich
Carboxypeptidase A−Agarose, ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas