1nb1

From Proteopedia

(Difference between revisions)

Revision as of 18:02, 24 December 2014

High resolution solution structure of kalata B1

Structural highlights

1nb1 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
Resources:	FirstGlance, OCA, 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

In recent years an increasing number of miniproteins containing an amide-cyclized backbone have been discovered. The cyclotide family is the largest group of such proteins and is characterized by a circular protein backbone and six conserved cysteine residues linked by disulfide bonds in a tight core of the molecule. These form a cystine knot in which an embedded ring formed by two of the disulfide bonds and the connecting backbone segment is threaded by a third disulfide bond. In the current study we have undertaken high resolution structural analysis of two prototypic cyclotides, kalata B1 and cycloviolacin O1, to define the role of the conserved residues in the sequence. We provide the first comprehensive analysis of the topological features in this unique family of proteins, namely rings (a circular backbone), twists (a cis-peptide bond in the Mobius cyclotides) and knots (a knotted arrangement of the disulfide bonds).

Twists, knots, and rings in proteins. Structural definition of the cyclotide framework.,Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:12482868^[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
↑ Rosengren KJ, Daly NL, Plan MR, Waine C, Craik DJ. Twists, knots, and rings in proteins. Structural definition of the cyclotide framework. J Biol Chem. 2003 Mar 7;278(10):8606-16. Epub 2002 Dec 12. PMID:12482868 doi:10.1074/jbc.M211147200

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/1nb1"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1nb1]] 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=1NB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NB1 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kal|1kal]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kal|1kal]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nb1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nb1 RCSB], [http://www.ebi.ac.uk/pdbsum/1nb1 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=1nb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nb1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nb1 RCSB], [http://www.ebi.ac.uk/pdbsum/1nb1 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://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 ==
@@ Line 19: / Line 21: @@
 </StructureSection>
 [[Category: Oldenlandia affinis]]
-[[Category: Craik, D J.]]
+[[Category: Craik, D J]]
-[[Category: Daly, N L.]]
+[[Category: Daly, N L]]
-[[Category: Plan, M R.]]
+[[Category: Plan, M R]]
-[[Category: Rosengren, K J.]]
+[[Category: Rosengren, K J]]
-[[Category: Waine, C.]]
+[[Category: Waine, C]]
 [[Category: Antibiotic]]
 [[Category: Cck]]

1nb1

From Proteopedia

Revision as of 18:02, 24 December 2014

High resolution solution structure of kalata B1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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