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1df0

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[[Image:1df0.gif|left|200px]]<br /><applet load="1df0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1df0.gif|left|200px]]
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caption="1df0, resolution 2.6&Aring;" />
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'''CRYSTAL STRUCTURE OF M-CALPAIN'''<br />
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{{Structure
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|PDB= 1df0 |SIZE=350|CAPTION= <scene name='initialview01'>1df0</scene>, resolution 2.6&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF M-CALPAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DF0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.52 and 3.4.22.53 3.4.22.52 and 3.4.22.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA].
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1DF0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DF0 OCA].
==Reference==
==Reference==
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Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation., Hosfield CM, Elce JS, Davies PL, Jia Z, EMBO J. 1999 Dec 15;18(24):6880-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10601010 10601010]
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Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation., Hosfield CM, Elce JS, Davies PL, Jia Z, EMBO J. 1999 Dec 15;18(24):6880-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10601010 10601010]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: zymogen activation]]
[[Category: zymogen activation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:29 2008''

Revision as of 08:37, 20 March 2008

Image:1df0.gif


PDB ID 1df0

Drag the structure with the mouse to rotate
, resolution 2.6Å
Activity: Hydrolase, with EC number and 3.4.22.53 3.4.22.52 and 3.4.22.53
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF M-CALPAIN


Overview

The combination of thiol protease activity and calmodulin-like EF-hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of the Ca(2+)-induced switch between inactive and active forms has remained elusive in the absence of structural information. We describe here the 2.6 A crystal structure of m-calpain in the Ca(2+)-free form, which illustrates the structural basis for the inactivity of calpain in the absence of Ca(2+). It also reveals an unusual thiol protease fold, which is associated with Ca(2+)-binding domains through heterodimerization and a C(2)-like beta-sandwich domain. Strikingly, the structure shows that the catalytic triad is not assembled, indicating that Ca(2+)-binding must induce conformational changes that re-orient the protease domains to form a functional active site. The alpha-helical N-terminal anchor of the catalytic subunit does not occupy the active site but inhibits its assembly and regulates Ca(2+)-sensitivity through association with the regulatory subunit. This Ca(2+)-dependent activation mechanism is clearly distinct from those of classical proteases.

About this Structure

1DF0 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation., Hosfield CM, Elce JS, Davies PL, Jia Z, EMBO J. 1999 Dec 15;18(24):6880-9. PMID:10601010

Page seeded by OCA on Thu Mar 20 10:37:29 2008

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