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Protein Domain : Peptidase M41-like

Primary Identifier  IPR037219 Type  Homologous_superfamily
Short Name  Peptidase_M41-like
description  Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role. Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].This group of metallopeptidases belong to MEROPS peptidase family M41 (FtsH endopeptidase family, clan MA(E)). The predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH.The peptidase M41 family belong to a larger family of zinc metalloproteases. This familyincludes the cell division protein FtsH, and the yeast mitochondrial respiratory chain complexesassembly protein, which is a putative ATP-dependent protease required for assembly of themitochondrial respiratory chain and ATPase complexes. FtsH is an integral membrane protein,which seems to act as an ATP-dependent zinc metallopeptidase that binds one zinc ion.

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0 Parent Features

24 Protein Domain Regions