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. 2011 Jan 21;107(7):1171–1181. doi: 10.1093/aob/mcq265

Fig. 1.

Fig. 1.

Organization and structures of M1 metallopeptidases. (A) Pictogram of an M1 metalloprotease showing the enzymatic domains (light blue), hydrophobic domain (dark blue) and protein–protein interaction domains (magenta). The zinc-binding amino acids are highlighted in red. (B) Crystal structures (from the Research Collaboratory for Structural Bioinformatics Protein Database) of M1 metallopeptidases: Escherichia coli aminopeptidase N (pepN) in complex with phenylalanine (3B34) (Addlagatta et al., 2008); tricorn interacting factor F3 from Thermoplasma acidophilum (1Z5H ) (Kyrieleis et al., 2005); soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1 (2XDT) (Vollmar et al., 2010); LTA4H in complex with Arg-Ala-Arg substrate (3B7T) (Tholander et al., 2008). The zinc ion is represented by a blue (pepN, ERAP) or grey (tricorn F3, LTA4H) sphere.