1m72: Difference between revisions
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[[Image:1m72.gif|left|200px]] | [[Image:1m72.gif|left|200px]] | ||
'''Crystal Structure of Caspase-1 from Spodoptera frugiperda''' | {{Structure | ||
|PDB= 1m72 |SIZE=350|CAPTION= <scene name='initialview01'>1m72</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Caspase-1 Caspase-1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.36 3.4.22.36] | |||
|GENE= | |||
}} | |||
'''Crystal Structure of Caspase-1 from Spodoptera frugiperda''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1M72 is a [ | 1M72 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M72 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of an invertebrate caspase., Forsyth CM, Lemongello D, LaCount DJ, Friesen PD, Fisher AJ, J Biol Chem. 2004 Feb 20;279(8):7001-8. Epub 2003 Nov 27. PMID:[http:// | Crystal structure of an invertebrate caspase., Forsyth CM, Lemongello D, LaCount DJ, Friesen PD, Fisher AJ, J Biol Chem. 2004 Feb 20;279(8):7001-8. Epub 2003 Nov 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14645217 14645217] | ||
[[Category: Caspase-1]] | [[Category: Caspase-1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:44 2008'' | ||
Revision as of 13:39, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Caspase-1, with EC number 3.4.22.36 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Caspase-1 from Spodoptera frugiperda
OverviewOverview
Caspases play an essential role in the execution of apoptosis. These cysteine proteases are highly conserved among metazoans and are translated as inactive zymogens, which are activated by proteolytic cleavages to generate the large and small subunits and remove the N-terminal prodomain. The 2.3 A resolution crystal structure of active Sf-caspase-1, the principal effector caspase of the insect Spodoptera frugiperda, is presented here. The structure represents the first nonhuman caspase to be resolved. The structure of the cleaved and active protease was determined with the tetrapeptide inhibitor N-acetyl-Asp-Glu-Val-Asp-chloromethylketone covalently bonded to the active site cysteine. As expected, the overall fold of Sf-caspase-1 is exceedingly similar to that of the five active caspases from humans solved to date. The overall structure and active site arrangement of Sf-caspase-1 is most comparable with that of the human effector caspases, with which it shares highest sequence homology. The most prominent structural difference with Sf-caspase-1 is the position of the N-terminal region of the large subunit. Unlike the N terminus of human caspases, the N terminus of Sf-caspase-1 originates from the active site side where it interacts with active site loop L2 and then extends to the backside of the heterodimer. This unusual structural arrangement raises the possibility that the N-terminal prodomain plays a regulatory role during effector caspase activation or enzyme activity in insects.
About this StructureAbout this Structure
1M72 is a Single protein structure of sequence from Spodoptera frugiperda. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of an invertebrate caspase., Forsyth CM, Lemongello D, LaCount DJ, Friesen PD, Fisher AJ, J Biol Chem. 2004 Feb 20;279(8):7001-8. Epub 2003 Nov 27. PMID:14645217
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