Protein Family Models

PreP is a protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. This entry represents the C-terminal domain of PreP and related proteins. Paper describing PDB structure 2fge. [1]. 16601675. The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis. Johnson KA, Bhushan S, Stahl A, Hallberg BM, Frohn A, Glaser E, Eneqvist T;. EMBO J. 2006;25:1977-1986. Paper describing PDB structure 4l3t. [2]. 24931469. Molecular basis of substrate recognition and degradation by human presequence protease. King JV, Liang WG, Scherpelz KP, Schilling AB, Meredith SC, Tang WJ;. Structure. 2014;22:996-1007. Paper describing PDB structure 6xos. [3]. 35383169. Structural basis for the mechanisms of human presequence protease conformational switch and substrate recognition. Liang WG, Wijaya J, Wei H, Noble AJ, Mancl JM, Mo S, Lee D, Lin King JV, Pan M, Liu C, Koehler CM, Zhao M, Potter CS, Carragher B, Li S, Tang WJ;. Nat Commun. 2022;13:1833. (from Pfam)

Date:

2024-10-16

This domain appears in eukaryotes as well as bacteria and tends to be found near the C-terminus of the metalloprotease M16C (Pfam:PF05193). (from Pfam)

Date:

2024-08-14

Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp [1]. [1]. 11470436. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J;. Structure (Camb) 2001;9:615-625. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

insulinase family protein (peptidase M16) is a zinc-dependent peptidase that cleaves small peptides close to a terminus, often including bonds on the amino side of basic residues such as arginine

Date:

2017-11-28