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1m72

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(New page: 200px<br /><applet load="1m72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m72, resolution 2.30&Aring;" /> '''Crystal Structure of...)
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[[Image:1m72.gif|left|200px]]<br /><applet load="1m72" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m72, resolution 2.30&Aring;" />
 
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'''Crystal Structure of Caspase-1 from Spodoptera frugiperda'''<br />
 
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==Overview==
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==Crystal Structure of Caspase-1 from Spodoptera frugiperda==
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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.
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<StructureSection load='1m72' size='340' side='right'caption='[[1m72]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m72]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M72 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m72 OCA], [https://pdbe.org/1m72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m72 RCSB], [https://www.ebi.ac.uk/pdbsum/1m72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m72 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CASP1_SPOFR CASP1_SPOFR]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/1m72_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1m72 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spodoptera_frugiperda Spodoptera frugiperda] with ACE and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M72 OCA].
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*[[Caspase 3D structures|Caspase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14645217 14645217]
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[[Category: Large Structures]]
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[[Category: Caspase-1]]
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[[Category: Single protein]]
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[[Category: Spodoptera frugiperda]]
[[Category: Spodoptera frugiperda]]
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[[Category: Fisher, A.J.]]
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[[Category: Fisher AJ]]
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[[Category: Forsyth, C.M.]]
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[[Category: Forsyth CM]]
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[[Category: Friesen, P.D.]]
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[[Category: Friesen PD]]
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[[Category: Lemongello, D.]]
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[[Category: Lemongello D]]
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[[Category: ACE]]
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[[Category: EDO]]
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[[Category: caspase]]
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[[Category: cysteine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:11:49 2007''
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Current revision

Crystal Structure of Caspase-1 from Spodoptera frugiperda

PDB ID 1m72

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