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==Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)== | |||
<StructureSection load='4xoj' size='340' side='right'caption='[[4xoj]], [[Resolution|resolution]] 0.91Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xoj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOJ 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]] 0.91Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xoj OCA], [https://pdbe.org/4xoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xoj RCSB], [https://www.ebi.ac.uk/pdbsum/4xoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xoj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serine proteinase catalyzed peptide splicing was demonstrated in both, one and two-peptide-chain (C- and N-terminal peptide chains linked by a disulfide bridge) trypsin inhibitor SFTI-1 analogues. In the second series, peptide splicing, with catalytic amount of proteinase, was observed only when formation of acyl-enzyme intermediate was preceded by the hydrolysis of the substrate Lys-Ser peptide bond. Here we presented that at an equimolar amount of the proteinase, splicing occurred in all two-peptide-chain analogues. This conclusion was supported by high resolution crystal structures of selected analogues in complex with trypsin. We showed that the process followed a direct transpeptidation mechanism. It means that the acyl-enzyme intermediate was formed and was immediately utilized for a new peptide bond formation, and products associated with the hydrolysis of acyl-enzyme were not observed. The demonstrated peptide splicing was a sequence- not structure-specific. | |||
Investigation of serine proteinase catalyzed peptide splicing in analogues of sunflower trypsin inhibitor 1 (SFTI-1).,Karna N, Malicki S, Debowski D, Golik P, Gitlin A, Grudnik P, Wladyka B, Brzozowski K, Dubin G, Rolka K, Legowska A Chembiochem. 2015 Jul 25. doi: 10.1002/cbic.201500296. PMID:26212347<ref>PMID:26212347</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4xoj" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Brzozowski | ==See Also== | ||
[[Category: | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
[[Category: | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Legowska | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Helianthus annuus]] | ||
[[Category: Large Structures]] | |||
[[Category: Brzozowski K]] | |||
[[Category: Debowski D]] | |||
[[Category: Dubin G]] | |||
[[Category: Gitlin A]] | |||
[[Category: Golik P]] | |||
[[Category: Grudnik P]] | |||
[[Category: Karna N]] | |||
[[Category: Legowska A]] | |||
[[Category: Malicki S]] | |||
[[Category: Rolka K]] | |||
[[Category: Wladyka B]] | |||
Latest revision as of 13:50, 10 January 2024
Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)
Structural highlights
FunctionPublication Abstract from PubMedSerine proteinase catalyzed peptide splicing was demonstrated in both, one and two-peptide-chain (C- and N-terminal peptide chains linked by a disulfide bridge) trypsin inhibitor SFTI-1 analogues. In the second series, peptide splicing, with catalytic amount of proteinase, was observed only when formation of acyl-enzyme intermediate was preceded by the hydrolysis of the substrate Lys-Ser peptide bond. Here we presented that at an equimolar amount of the proteinase, splicing occurred in all two-peptide-chain analogues. This conclusion was supported by high resolution crystal structures of selected analogues in complex with trypsin. We showed that the process followed a direct transpeptidation mechanism. It means that the acyl-enzyme intermediate was formed and was immediately utilized for a new peptide bond formation, and products associated with the hydrolysis of acyl-enzyme were not observed. The demonstrated peptide splicing was a sequence- not structure-specific. Investigation of serine proteinase catalyzed peptide splicing in analogues of sunflower trypsin inhibitor 1 (SFTI-1).,Karna N, Malicki S, Debowski D, Golik P, Gitlin A, Grudnik P, Wladyka B, Brzozowski K, Dubin G, Rolka K, Legowska A Chembiochem. 2015 Jul 25. doi: 10.1002/cbic.201500296. PMID:26212347[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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