4xoj: Difference between revisions
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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 [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XOJ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></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=4xoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xoj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xoj RCSB], [http://www.ebi.ac.uk/pdbsum/4xoj PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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;"> | |||
== 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> | |||
</div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Trypsin]] | |||
[[Category: Brzozowski, K]] | [[Category: Brzozowski, K]] | ||
[[Category: Debowski, D]] | [[Category: Debowski, D]] | ||
[[Category: Dubin, G]] | [[Category: Dubin, G]] | ||
[[Category: Gitlin, A]] | |||
[[Category: Golik, P]] | |||
[[Category: Grudnik, P]] | |||
[[Category: Karna, N]] | |||
[[Category: Legowska, A]] | [[Category: Legowska, A]] | ||
[[Category: Malicki, S]] | |||
[[Category: Rolka, K]] | |||
[[Category: Wladyka, B]] | [[Category: Wladyka, B]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Inhibitor]] | ||
[[Category: Protease]] | |||
[[Category: Sfti]] | |||
[[Category: Splicing]] | |||
Revision as of 17:37, 12 August 2015
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
Function[SFTI1_HELAN] Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.[1] Publication 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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