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| - | ==SOLUTION STRUCTURE OF SFTI-1(6,5), AN ACYCLIC PERMUTANT OF THE PROTEINASE INHIBITOR SFTI-1, TRANS-TRANS-TRANS CONFORMER (TT-A)== | + | |
| - | <StructureSection load='1o8y' size='340' side='right' caption='[[1o8y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | ==Solution structure of SFTI-1(6,5), an acyclic permutant of the proteinase inhibitor SFTI-1, trans-trans-trans conformer (tt-A)== |
| | + | <StructureSection load='1o8y' size='340' side='right'caption='[[1o8y]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1o8y]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O8Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1o8y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jbl|1jbl]], [[1jbn|1jbn]], [[1o8z|1o8z]], [[1sfi|1sfi]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1o8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o8y RCSB], [http://www.ebi.ac.uk/pdbsum/1o8y PDBsum]</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=1o8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8y OCA], [https://pdbe.org/1o8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o8y RCSB], [https://www.ebi.ac.uk/pdbsum/1o8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SFTI1_HELAN SFTI1_HELAN] Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.<ref>PMID:10390350</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1o8y" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Trypsin inhibitor|Trypsin inhibitor]] | + | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Craik, D J]] | + | [[Category: Helianthus annuus]] |
| - | [[Category: Marx, U C]] | + | [[Category: Large Structures]] |
| - | [[Category: Acyclic permutant]] | + | [[Category: Craik DJ]] |
| - | [[Category: Bowman-birk inhibitor]] | + | [[Category: Marx UC]] |
| - | [[Category: Protease inhibitor]]
| + | |
| - | [[Category: Sfti-1]]
| + | |
| Structural highlights
Function
SFTI1_HELAN Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.[1]
Publication Abstract from PubMed
The most potent known naturally occurring Bowman-Birk inhibitor, sunflower trypsin inhibitor-1 (SFTI-1), is a bicyclic 14-amino acid peptide from sunflower seeds comprising one disulfide bond and a cyclic backbone. At present, little is known about the cyclization mechanism of SFTI-1. We show here that an acyclic permutant of SFTI-1 open at its scissile bond, SFTI-1[6,5], also functions as an inhibitor of trypsin and that it can be enzymatically backbone-cyclized by incubation with bovine beta-trypsin. The resulting ratio of cyclic SFTI-1 to SFTI-1[6,5] is approximately 9:1 regardless of whether trypsin is incubated with SFTI-1[6,5] or SFTI-1. Enzymatic resynthesis of the scissile bond to form cyclic SFTI-1 is a novel mechanism of cyclization of SFTI-1[6,5]. Such a reaction could potentially occur on a trypsin affinity column as used in the original isolation procedure of SFTI-1. We therefore extracted SFTI-1 from sunflower seeds without a trypsin purification step and confirmed that the backbone of SFTI-1 is indeed naturally cyclic. Structural studies on SFTI-1[6,5] revealed high heterogeneity, and multiple species of SFTI-1[6,5] were identified. The main species closely resembles the structure of cyclic SFTI-1 with the broken binding loop able to rotate between a cis/trans geometry of the I7-P8 bond with the cis conformer being similar to the canonical binding loop conformation. The non-reactive loop adopts a beta-hairpin structure as in cyclic wild-type SFTI-1. Another species exhibits an iso-aspartate residue at position 14 and provides implications for possible in vivo cyclization mechanisms.
Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide.,Marx UC, Korsinczky ML, Schirra HJ, Jones A, Condie B, Otvos L Jr, Craik DJ J Biol Chem. 2003 Jun 13;278(24):21782-9. Epub 2003 Mar 5. PMID:12621047[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Luckett S, Garcia RS, Barker JJ, Konarev AV, Shewry PR, Clarke AR, Brady RL. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J Mol Biol. 1999 Jul 9;290(2):525-33. PMID:10390350 doi:10.1006/jmbi.1999.2891
- ↑ Marx UC, Korsinczky ML, Schirra HJ, Jones A, Condie B, Otvos L Jr, Craik DJ. Enzymatic cyclization of a potent bowman-birk protease inhibitor, sunflower trypsin inhibitor-1, and solution structure of an acyclic precursor peptide. J Biol Chem. 2003 Jun 13;278(24):21782-9. Epub 2003 Mar 5. PMID:12621047 doi:10.1074/jbc.M212996200
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