1r6v
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(New page: 200px<br /><applet load="1r6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6v, resolution 1.7Å" /> '''Crystal structure of ...)
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Revision as of 20:07, 24 November 2007
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Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin
Overview
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.
About this Structure
1R6V is a Single protein structure of sequence from Fervidobacterium pennivorans with CA as ligand. Full crystallographic information is available from OCA.
Reference
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 Jan 16;335(3):787-97. PMID:14687574
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