We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
1znu
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1znu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1znu" /> '''Structure of cyclotide Kalata B1 in DPC mice...) |
|||
| (15 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1znu.gif|left|200px]]<br /><applet load="1znu" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1znu" /> | ||
| - | '''Structure of cyclotide Kalata B1 in DPC micelles solution'''<br /> | ||
| - | == | + | ==Structure of cyclotide Kalata B1 in DPC micelles solution== |
| - | Cyclotides are a family of bioactive plant peptides that are characterized | + | <StructureSection load='1znu' size='340' side='right'caption='[[1znu]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1znu]] 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=1ZNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZNU FirstGlance]. <br> | ||
| + | </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=1znu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znu OCA], [https://pdbe.org/1znu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1znu RCSB], [https://www.ebi.ac.uk/pdbsum/1znu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1znu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cyclotides are a family of bioactive plant peptides that are characterized by a circular protein backbone and three conserved tightly packed disulfide bonds. The antimicrobial and hemolytic properties of cyclotides, along with the relative hydrophobicity of the peptides, point to the biological membrane as a target for cyclotides. To assess the membrane-induced conformation and orientation of cyclotides, the interaction of the Mobius cyclotide, kalata B1, from the African perennial plant Oldenlandia affinis, with dodecylphosphocholine micelles was studied using NMR spectroscopy. Under conditions where the cyclotide formed a well-defined complex with micelles, the spatial structure of kalata B1 was calculated from NOE and J couplings data, and the model for the peptide-micelle complex was built using 5- and 16-doxylstearate relaxation probes. The binding of divalent cations to the peptide-micelle complex was quantified by Mn2+ titration. The results show that the peptide binds to the micelle surface, with relatively high affinity, via two hydrophobic loops (loop 5, Trp19-Val21; and loop6, Leu27-Val29). The charged residues (Glu3 and Arg24), along with the cation-binding site (near Glu3) are segregated on the other side of the molecule and in contact with polar head groups of detergent. The spatial structure of kalata B1 is only slightly changed during incorporation into micelles and represents a distorted triple-stranded beta-sheet cross-linked by a cystine knot. Detailed structural analysis and comparison with other knottins revealed structural conservation of the two-disulfide motif in cyclic and acyclic peptides. The results thus obtained provide the first model for interaction of cyclotides with membranes and permit consideration of the cyclotides as membrane-active cationic antimicrobial peptides. | ||
| - | + | Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle.,Shenkarev ZO, Nadezhdin KD, Sobol VA, Sobol AG, Skjeldal L, Arseniev AS FEBS J. 2006 Jun;273(12):2658-72. PMID:16817894<ref>PMID:16817894</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1znu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Oldenlandia affinis]] | [[Category: Oldenlandia affinis]] | ||
| - | + | [[Category: Arseniev AS]] | |
| - | [[Category: Arseniev | + | [[Category: Nadezhdin KD]] |
| - | [[Category: Nadezhdin | + | [[Category: Shenkarev ZO]] |
| - | [[Category: Shenkarev | + | [[Category: Skjeldal L]] |
| - | [[Category: Skjeldal | + | [[Category: Sobol AG]] |
| - | [[Category: Sobol | + | [[Category: Sobol VA]] |
| - | [[Category: Sobol | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Structure of cyclotide Kalata B1 in DPC micelles solution
| |||||||||||
