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| | ==REFINED STRUCTURE AND DISULFIDE PAIRING OF THE KALATA B1 PEPTIDE== | | ==REFINED STRUCTURE AND DISULFIDE PAIRING OF THE KALATA B1 PEPTIDE== |
| - | <StructureSection load='1jjz' size='340' side='right'caption='[[1jjz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1jjz' size='340' side='right'caption='[[1jjz]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jjz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oldenlandia_affinis Oldenlandia affinis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JJZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jjz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oldenlandia_affinis Oldenlandia affinis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kal|1kal]]</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://proteopedia.org/fgij/fg.htm?mol=1jjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjz OCA], [http://pdbe.org/1jjz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jjz RCSB], [http://www.ebi.ac.uk/pdbsum/1jjz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjz ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_000749:KALATA+B1'>PRD_000749</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=1jjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjz OCA], [https://pdbe.org/1jjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjz RCSB], [https://www.ebi.ac.uk/pdbsum/1jjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KAB4_OLDAF KAB4_OLDAF]] Probably participates in a plant defense mechanism. | + | [https://www.uniprot.org/uniprot/KAB1_OLDAF KAB1_OLDAF] Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.<ref>PMID:17534989</ref> <ref>PMID:12779323</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oldenlandia affinis]] | | [[Category: Oldenlandia affinis]] |
| - | [[Category: Gran, L]] | + | [[Category: Gran L]] |
| - | [[Category: Skjeldal, L]] | + | [[Category: Skjeldal L]] |
| - | [[Category: Sletten, K]] | + | [[Category: Sletten K]] |
| - | [[Category: Volkman, B F]] | + | [[Category: Volkman BF]] |
| - | [[Category: Cyclic peptide]]
| + | |
| - | [[Category: Cyclotide]]
| + | |
| - | [[Category: Disulfide pairing]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Uterotonic]]
| + | |
| Structural highlights
Function
KAB1_OLDAF Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.[1] [2]
Publication Abstract from PubMed
The cyclic polypeptide kalata B1 from the African plant Oldenlandia affinis DC consists of 29 amino acid residues with three disulfide linkages. In this study we used two-dimensional NMR spectroscopy to investigate the three-dimensional structure of the peptide and to determine the disulfide connectivities. Nuclear Overhauser effects (NOEs) between neighboring beta-protons of the cysteines detected at 750 MHz provided evidence for the disulfide connectivity pattern 5-13, 17-29, and 22-27. These disulfide linkages were confirmed by three-dimensional structures calculated from input constraints derived solely from NOEs without explicit disulfide connectivities. Kalata B1 is insoluble in aqueous solution above pH 3.5, but in a 50-50 water-methanol mixture, it was possible to use natural abundance two-dimensional (15)N-(1)H heteronuclear single quantum coherence spectroscopy to study the hydrophobic peptide from pH 2 to 10. The addition of methanol resulted in no significant structural changes. Although the peptide contains three prolyl residues, no evidence of multiple conformers was detected at any pH. The addition of Mn(2+) to kalata B1 resulted in selective broadening of resonances from Asn 23, Thr 24, and Glu 15; these results suggest that these three residues are involved in a specific metal binding site.
Refined structure and metal binding site of the kalata B1 peptide.,Skjeldal L, Gran L, Sletten K, Volkman BF Arch Biochem Biophys. 2002 Mar 15;399(2):142-8. PMID:11888199[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Plan MR, Goransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. Chembiochem. 2007 Jun 18;8(9):1001-11. PMID:17534989 doi:http://dx.doi.org/10.1002/cbic.200700097
- ↑ Barry DG, Daly NL, Clark RJ, Sando L, Craik DJ. Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity. Biochemistry. 2003 Jun 10;42(22):6688-95. PMID:12779323 doi:http://dx.doi.org/10.1021/bi027323n
- ↑ Skjeldal L, Gran L, Sletten K, Volkman BF. Refined structure and metal binding site of the kalata B1 peptide. Arch Biochem Biophys. 2002 Mar 15;399(2):142-8. PMID:11888199 doi:10.1006/abbi.2002.2769
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