3i74
From Proteopedia
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| - | {{STRUCTURE_3i74| PDB=3i74 | SCENE= }} | ||
| - | ===Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor=== | ||
| - | {{ABSTRACT_PUBMED_19805099}} | ||
| - | == | + | ==Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor== |
| - | [[3i74]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3i74' size='340' side='right'caption='[[3i74]], [[Resolution|resolution]] 2.60Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3i74]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I74 FirstGlance]. <br> | ||
| + | </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> | ||
| + | <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=ALV:(2S)-2-AMINOPROPANE-1,1-DIOL'>ALV</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=3i74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i74 OCA], [https://pdbe.org/3i74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i74 RCSB], [https://www.ebi.ac.uk/pdbsum/3i74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i74 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SBT3_SOLLC SBT3_SOLLC] Serine protease (PubMed:19332543, PubMed:19407393, PubMed:19805099, PubMed:27259555, PubMed:27451395). Has preference for Gln in the P1 position and Lys in the P2 position of oligopeptide substrates. Active also with His in the P1 position (PubMed:19332543). Involved in resistance against insects partly by regulating expression of systemic wound response genes and possibly by its post-ingestive activity in the insect gut. Apart from the role in defense, may be involved in regulation of pectin methylesterases (PMEs) activity and pectin methylesterification of the cell wall (PubMed:27259555).<ref>PMID:19332543</ref> <ref>PMID:19407393</ref> <ref>PMID:19805099</ref> <ref>PMID:27259555</ref> <ref>PMID:27451395</ref> | ||
| + | == 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/i7/3i74_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3i74 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Subtilases are serine proteases found in Archae, Bacteria, yeasts, and higher eukaryotes. Plants possess many more of these subtilisin-like endopeptidases than animals, e.g., 56 identified genes in Arabidopsis compared with only 9 in humans, indicating important roles for subtilases in plant biology. We report the first structure of a plant subtilase, SBT3 from tomato, in the active apo form and complexed with a chloromethylketone (cmk) inhibitor. The domain architecture comprises an N-terminal protease domain displaying a 132 aa protease-associated (PA) domain insertion and a C-terminal seven-stranded jelly-roll fibronectin (Fn) III-like domain. We present the first structural evidence for an explicit function of PA domains in proteases revealing a vital role in the homo-dimerization of SBT3 and in enzyme activation. Although Ca(2+)-binding sites are conserved and critical for stability in other subtilases, SBT3 was found to be Ca(2+)-free and its thermo stability is Ca(2+)-independent. | ||
| - | + | Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.,Ottmann C, Rose R, Huttenlocher F, Cedzich A, Hauske P, Kaiser M, Huber R, Schaller A Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):17223-8. Epub 2009 Sep 23. PMID:19805099<ref>PMID:19805099</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3i74" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Solanum lycopersicum]] | [[Category: Solanum lycopersicum]] | ||
| - | [[Category: Ottmann | + | [[Category: Ottmann C]] |
| - | [[Category: Rose | + | [[Category: Rose R]] |
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Current revision
Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor
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