Issue 4, 2012

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

Abstract

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.

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

Supplementary files

Article information

Article type
Paper
Submitted
10 Jan 2012
Accepted
14 Feb 2012
First published
05 Mar 2012

Metallomics, 2012,4, 379-388

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