Protein Family Models

The founding member of this family is the N-terminal prodomain of fervidolysin, an extracellular subtilisin-like serine protease. This domain folds into a globular alpha/beta structure consisting of four-stranded antiparallel beta-sheet and two alpha-helices packed on one side of it [1]. The prodomain is proteolytically cleaved and removed from the proenzyme. Paper describing PDB structure 1r6v. [1]. 14687574. Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin. Kim JS, Kluskens LD, de Vos WM, Huber R, van der Oost J;. J Mol Biol. 2004;335:787-797. (from Pfam)

Date:

2024-10-28

This is the N-terminal domain found in ORF 2 (open reading frame 2), a protein encoded just downstream of asp (A. sobria serine protease). The ORF 2 N-terminal domain is essential for proper ASP folding. This domain is intrinsically disordered but forms some degree of secondary structure upon binding ASP [1, 2]. [1]. 25784551. Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria. Kobayashi H, Yoshida T, Miyakawa T, Tashiro M, Okamoto K, Yamanaka H, Tanokura M, Tsuge H;. J Biol Chem. 2015;290:11130-11143. [2]. 29023605. Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity. Kobayashi H, Otsubo T, Teraoka F, Ikeda K, Seike S, Takahashi E, Okamoto K, Yoshida T, Tsuge H, Yamanaka H;. PLoS One. 2017;12:e0186392. (from Pfam)

Date:

2024-10-16