Protein Family Models

This domain is found in Xaa-Pro dipeptidase from Escherichia coli (PepQ), a metalloprotease that catalyse the cleavage of Xaa-Pro dipeptides. This protein is organised into N-terminal (this entry) and C-terminal (usually Pfam:PF00557) domains and adopts a dimeric configuration. This domain shows an alpha-beta structure with four helices, one pair flanking each side of the six-stranded mixed beta-sheet [1-5]. Paper describing PDB structure 3l24. [1]. 20000741. Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase. Vyas NK, Nickitenko A, Rastogi VK, Shah SS, Quiocho FA;. Biochemistry. 2010;49:547-559. Paper describing PDB structure 3rva. [2]. 23545636. Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases. Stepankova A, Duskova J, Skalova T, Hasek J, Koval' T, Ostergaard LH, Dohnalek J;. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013;69:346-354. Paper describing PDB structure 4qr8. [3]. 25354344. Structural basis of substrate selectivity of E. coli prolidase. Weaver J, Watts T, Li P, Rye HS;. PLoS One. 2014;9:e111531. Paper describing PDB structure 4zwo. [4]. 26418828. Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX. Daczkowski CM, Pegan SD, Harvey SP;. Biochemistry. 2015;54:6423-6433. Paper describing PDB structure 6ah7. [5]. 32515491. Repurposing a bacterial prolidase for organophosphorus hydrolysis: Reshaped catalytic cavity switches substrate selectivity. Yang J, Xiao YZ, Li R, Liu Y, Long LJ;. Biote. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3]. The structure of a representative of this family. [1]. 8471602. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Roderick SL, Matthews BW. Biochemistry 1993;32:3907-3912. -!- Members of this family are metallopeptidases. They belong to family M24 in the classification of Rawlings and Barrett. [2]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. [3]. 18579787. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Stuwe T, Hothorn M, Lejeune E, Rybin V, Bortfeld M, Scheffzek K, Ladurner AG;. Proc Natl Acad Sci U S A. 2008;105:8884-8889. (from Pfam)

Date:

2024-10-16

aminopeptidase family protein P (peptidase M24) cleaves amido-, imido- or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Date:

2017-06-22

Gene:

pepQ

Date:

2020-10-26