1r6v
From Proteopedia
(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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1r6v.gif|left|200px]]<br /><applet load="1r6v" size=" | + | [[Image:1r6v.gif|left|200px]]<br /><applet load="1r6v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r6v, resolution 1.7Å" /> | caption="1r6v, resolution 1.7Å" /> | ||
'''Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin'''<br /> | '''Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structure-forming fibrous proteins like keratins, gelatins and collagens | + | 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== | ==About this Structure== | ||
| - | 1R6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fervidobacterium_pennivorans Fervidobacterium pennivorans] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fervidobacterium_pennivorans Fervidobacterium pennivorans] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6V OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
| - | [[Category: Kim, J | + | [[Category: Kim, J S.]] |
| - | [[Category: Kluskens, L | + | [[Category: Kluskens, L D.]] |
| - | [[Category: Oost, J | + | [[Category: Oost, J van der.]] |
| - | [[Category: Vos, W | + | [[Category: Vos, W M.de.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: propeptide]] | [[Category: propeptide]] | ||
| Line 23: | Line 23: | ||
[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:42 2008'' |
Revision as of 12:47, 21 February 2008
|
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 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
Page seeded by OCA on Thu Feb 21 14:47:42 2008
