3i74

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor

Structural highlights

3i74 is a 4 chain structure with sequence from Solanum lycopersicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4] ^[5]

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

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^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cedzich A, Huttenlocher F, Kuhn BM, Pfannstiel J, Gabler L, Stintzi A, Schaller A. The protease-associated domain and C-terminal extension are required for zymogen processing, sorting within the secretory pathway, and activity of tomato subtilase 3 (SlSBT3). J Biol Chem. 2009 May 22;284(21):14068-78. PMID:19332543 doi:10.1074/jbc.M900370200
↑ Rose R, Huttenlocher F, Cedzich A, Kaiser M, Schaller A, Ottmann C. Purification, crystallization and preliminary X-ray diffraction analysis of a plant subtilase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 May 1;65(Pt 5):522-5. PMID:19407393 doi:10.1107/S1744309109013979
↑ Ottmann C, Rose R, Huttenlocher F, Cedzich A, Hauske P, Kaiser M, Huber R, Schaller A. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):17223-8. Epub 2009 Sep 23. PMID:19805099
↑ Meyer M, Huttenlocher F, Cedzich A, Procopio S, Stroeder J, Pau-Roblot C, Lequart-Pillon M, Pelloux J, Stintzi A, Schaller A. The subtilisin-like protease SBT3 contributes to insect resistance in tomato. J Exp Bot. 2016 Jul;67(14):4325-38. PMID:27259555 doi:10.1093/jxb/erw220
↑ Meyer M, Leptihn S, Welz M, Schaller A. Functional Characterization of Propeptides in Plant Subtilases as Intramolecular Chaperones and Inhibitors of the Mature Protease. J Biol Chem. 2016 Sep 9;291(37):19449-61. PMID:27451395 doi:10.1074/jbc.M116.744151
↑ Ottmann C, Rose R, Huttenlocher F, Cedzich A, Hauske P, Kaiser M, Huber R, Schaller A. Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3. Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):17223-8. Epub 2009 Sep 23. PMID:19805099

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3i74"

Categories: Large Structures | Solanum lycopersicum | Ottmann C | Rose R

@@ Line 3: / Line 3: @@
 <StructureSection load='3i74' size='340' side='right'caption='[[3i74]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3i74]] is a 4 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=3I74 FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.6&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i6s|3i6s]]</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3i74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i74 OCA], [http://pdbe.org/3i74 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i74 RCSB], [http://www.ebi.ac.uk/pdbsum/3i74 PDBsum], [http://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]]
@@ Line 14: / Line 15: @@
   <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/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 34: / Line 35: @@
 [[Category: Large Structures]]
 [[Category: Solanum lycopersicum]]
-[[Category: Ottmann, C]]
+[[Category: Ottmann C]]
-[[Category: Rose, R]]
+[[Category: Rose R]]
-[[Category: Chloromethylketone inhibitor]]
-[[Category: Fn3-domain]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Pa-domain]]
-[[Category: Subtilisin-like protease]]

3i74

From Proteopedia

Current revision

Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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