1k48

From Proteopedia

(Difference between revisions)

Revision as of 14:03, 10 September 2015

REFINED STRUCTURE AND DISULFIDE PAIRING OF THE KALATA B1 PEPTIDE

Structural highlights

1k48 is a 1 chain structure with sequence from Oldenlandia affinis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1kal, 1jjz
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k48"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1k48]] 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=1K48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K48 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kal|1kal]], [[1jjz|1jjz]]</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=1k48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k48 RCSB], [http://www.ebi.ac.uk/pdbsum/1k48 PDBsum]</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=1k48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k48 OCA], [http://pdbe.org/1k48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k48 RCSB], [http://www.ebi.ac.uk/pdbsum/1k48 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1k48" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1k48

From Proteopedia

Revision as of 14:03, 10 September 2015

REFINED STRUCTURE AND DISULFIDE PAIRING OF THE KALATA B1 PEPTIDE

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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