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| [[Image:1df0.gif|left|200px]]
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| {{Structure
| | ==Crystal structure of M-Calpain== |
| |PDB= 1df0 |SIZE=350|CAPTION= <scene name='initialview01'>1df0</scene>, resolution 2.6Å
| | <StructureSection load='1df0' size='340' side='right'caption='[[1df0]], [[Resolution|resolution]] 2.60Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[1df0]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DF0 FirstGlance]. <br> |
| |ACTIVITY= <span class='plainlinks'>[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] </span>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| |GENE=
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [https://pdbe.org/1df0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB], [https://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1df0 ProSAT]</span></td></tr> |
| |DOMAIN=
| | </table> |
| |RELATEDENTRY=[[1aj5|1AJ5]], [[1alv|1ALV]], [[1alw|1ALW]], [[1dvi|1DVI]]
| | == Function == |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1df0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1df0 OCA], [http://www.ebi.ac.uk/pdbsum/1df0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1df0 RCSB]</span>
| | [https://www.uniprot.org/uniprot/CAN2_RAT CAN2_RAT] Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. |
| }}
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/df/1df0_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1df0 ConSurf]. |
| | <div style="clear:both"></div> |
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|
| '''CRYSTAL STRUCTURE OF M-CALPAIN'''
| | ==See Also== |
| | | *[[Calpain 3D structures|Calpain 3D structures]] |
| | | __TOC__ |
| ==Overview==
| | </StructureSection> |
| 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.
| | [[Category: Large Structures]] |
| | |
| ==About this Structure== | |
| 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].
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| ==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://www.ncbi.nlm.nih.gov/pubmed/10601010 10601010]
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| [[Category: Hydrolase]]
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| [[Category: Protein complex]] | |
| [[Category: Rattus norvegicus]] | | [[Category: Rattus norvegicus]] |
| [[Category: Davies, P L.]] | | [[Category: Davies PL]] |
| [[Category: Elce, J S.]] | | [[Category: Elce JS]] |
| [[Category: Hosfield, C M.]] | | [[Category: Hosfield CM]] |
| [[Category: Jia, Z.]] | | [[Category: Jia Z]] |
| [[Category: c2 domain]]
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| [[Category: calcium]]
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| [[Category: calmodulin]]
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| [[Category: calpain]]
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| [[Category: catalytic triad]]
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| [[Category: cysteine protease]]
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| [[Category: papain]]
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| [[Category: protease]]
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| [[Category: zymogen]]
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| [[Category: zymogen activation]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:18 2008''
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