1R6V

Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin

Summary for 1R6V

• Entry DOI: 10.2210/pdb1r6v/pdb
• Descriptor: subtilisin-like serine protease, CALCIUM ION (3 entities in total)
• Functional Keywords: subtilisin, sandwich domain, propeptide, hydrolase
• Biological source: Fervidobacterium pennivorans
• Total number of polymer chains: 1
• Total formula weight: 72038.53

Authors

Kim, J.S.,Kluskens, L.D.,de Vos, W.M.,Huber, R.,van der Oost, J. (deposition date: 2003-10-17, release date: 2004-10-19, Last modification date: 2024-02-14)

Primary citation

Kim, J.S.,Kluskens, L.D.,de Vos, W.M.,Huber, R.,van der Oost, J.
Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin.
J.Mol.Biol., 335:787-797, 2004

PubMed Abstract: Structure-forming fibrous proteins like keratins, gelatins and collagens are degraded only by a few proteases as their tight packing limits access to the potential cleavage sites. To understand the keratin degradation in detail, we describe the first crystal structure of a keratin-degrading enzyme (keratinase), fervidolysin, from Fervidobacterium pennivorans as an immature form with propeptide (PD)-bound. The 1.7A resolution crystal structure shows that the protease is composed of four domains: a catalytic domain (CD), two beta-sandwich domains (SDs), and the PD domain. A structural alignment shows a distant relationship between the PD-CD substructure of fervidolysin and pro-subtilisin E. Tight binding of PD to the remaining part of the protease is mediated by hydrogen bonds along the domain surfaces and around the active cleft, and by the clamps to SD1 and SD2. The crystal structure of this multi-domain protein fervidolysin provides insights into proenzyme activation and the role of non-catalytic domains, suggesting a functional relationship to the fibronectin (FN)-like domains of the human promatrix metalloprotease-2 (proMMP-2) that degrades the fibrous polymeric substrate gelatin.

PubMed: 14687574
DOI: 10.1016/j.jmb.2003.11.006

Experimental method

X-RAY DIFFRACTION (1.7 Å)