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| | ==CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+== | | ==CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+== |
| - | <StructureSection load='1aec' size='340' side='right' caption='[[1aec]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='1aec' size='340' side='right'caption='[[1aec]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1aec]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Actch Actch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AEC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1aec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinidia_chinensis Actinidia chinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AEC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Actinidain Actinidain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.14 3.4.22.14] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aec OCA], [http://pdbe.org/1aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aec RCSB], [http://www.ebi.ac.uk/pdbsum/1aec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aec ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aec OCA], [https://pdbe.org/1aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aec RCSB], [https://www.ebi.ac.uk/pdbsum/1aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aec ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACTN_ACTCH ACTN_ACTCH]] Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.<ref>PMID:18442249</ref> | + | [https://www.uniprot.org/uniprot/ACTN_ACTCC ACTN_ACTCC] Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.<ref>PMID:18442249</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/1aec_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ae/1aec_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actch]] | + | [[Category: Actinidia chinensis]] |
| - | [[Category: Actinidain]] | + | [[Category: Large Structures]] |
| - | [[Category: Varughese, K I]] | + | [[Category: Varughese KI]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
ACTN_ACTCC Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
E-64, 1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane, is a potent and highly selective irreversible inhibitor of cysteine proteases. The crystal structure of a complex of actinidin and E-64 has been determined at 1.86-A resolution by using the difference Fourier method and refined to an R-factor of 14.5%. The electron density map clearly shows that the C2 atom of the E-64 epoxide ring is covalently bonded to the S atom of the active-site cysteine 25. The charged carboxyl group of E-64 forms four H-bonds with the protein and thus may play an important role in favorably positioning the inhibitor molecule for nucleophilic attack by the active-site thiolate anion. The interaction features between E-64 and actinidin are very similar to those seen in the papain-E-64 complex; however, the amino-4-guanidinobutane group orients differently. The crystals of the actinidin-E-64 complex diffracted much better than the papain-E-64 complex, and consequently the present study provides more precise geometrical information on the binding of the inhibitor. Moreover, this study provides yet another confirmation that the binding of E-64 is at the S subsites and not at the S' subsites as has been previously proposed. The original actinidin structure has been revised using the new cDNA sequence information.
Crystal structure of an actinidin-E-64 complex.,Varughese KI, Su Y, Cromwell D, Hasnain S, Xuong NH Biochemistry. 1992 Jun 9;31(22):5172-6. PMID:1606141[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tuppo L, Giangrieco I, Palazzo P, Bernardi ML, Scala E, Carratore V, Tamburrini M, Mari A, Ciardiello MA. Kiwellin, a modular protein from green and gold kiwi fruits: evidence of in vivo and in vitro processing and IgE binding. J Agric Food Chem. 2008 May 28;56(10):3812-7. Epub 2008 Apr 29. PMID:18442249 doi:http://dx.doi.org/10.1021/jf703620m
- ↑ Varughese KI, Su Y, Cromwell D, Hasnain S, Xuong NH. Crystal structure of an actinidin-E-64 complex. Biochemistry. 1992 Jun 9;31(22):5172-6. PMID:1606141
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