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| - | [[Image:1o8z.jpg|left|200px]] | |
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| - | <!--
| + | ==Solution structure of SFTI-1(6,5), an acyclic permutant of the proteinase inhibitor SFTI-1, cis-trans-trans conformer (ct-A)== |
| - | The line below this paragraph, containing "STRUCTURE_1o8z", creates the "Structure Box" on the page.
| + | <StructureSection load='1o8z' size='340' side='right'caption='[[1o8z]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | + | <table><tr><td colspan='2'>[[1o8z]] 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=1O8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8Z FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </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'>[https://proteopedia.org/fgij/fg.htm?mol=1o8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8z OCA], [https://pdbe.org/1o8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o8z RCSB], [https://www.ebi.ac.uk/pdbsum/1o8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8z ProSAT]</span></td></tr> |
| - | {{STRUCTURE_1o8z| PDB=1o8z | SCENE= }}
| + | </table> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == 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. |
| | | | |
| - | '''SOLUTION STRUCTURE OF SFTI-1(6,5), AN ACYCLIC PERMUTANT OF THE PROTEINASE INHIBITOR SFTI-1, CIS-TRANS-TRANS CONFORMER (CT-A)'''
| + | 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<ref>PMID:12621047</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | 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.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1O8Z is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8Z OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1o8z" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12621047 12621047]
| + | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] |
| - | [[Category: Single protein]]
| + | == References == |
| - | [[Category: Craik, D J.]]
| + | <references/> |
| - | [[Category: Marx, U C.]] | + | __TOC__ |
| - | [[Category: Acyclic permutant]] | + | </StructureSection> |
| - | [[Category: Bowman-birk inhibitor]] | + | [[Category: Helianthus annuus]] |
| - | [[Category: Sfti-1]] | + | [[Category: Large Structures]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:32:17 2008''
| + | [[Category: Craik DJ]] |
| | + | [[Category: Marx UC]] |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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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