The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods

P. Kuhn, A. M. Deacon, S. Comoso, G. Rajaseger, R. M. Kini, I. Uson, Prasanna Kolatkar

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Bucandin is a novel presynaptic neurotoxin isolated from Bungarus candidus (Malayan krait). It has the unique property of enhancing presynaptic acetylcholine release and represents a family of three-finger toxins with an additional disulfide in the first loop. There are no existing structures from this sub-category of three-finger toxins. The X-ray crystal structure of bucandin has been determined by the Shake-and-Bake direct-methods procedure. The resulting electron-density maps were of outstanding quality and allowed the automated tracing of 61 of the 63 amino-acid residues, including their side chains, and the placement of 48 solvent molecules. The 0.97 Å resolution full-matrix least-squares refinement converged to a crystallographic R factor of 12.4% and the final model contains 118 solvent molecules. This is the highest resolution structure of any member of the three-finger toxin family and thus it can serve as the best model for other members of the family. Furthermore, the structure of this novel toxin will help in understanding its unique ability to enhance acetylcholine release. The unique structure resulting from the fifth disulfide bond residing in the first loop improves the understanding of other toxins with a similar arrangement of disulfide bonds.

Original languageEnglish
Pages (from-to)1401-1407
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number11
DOIs
Publication statusPublished - 29 Nov 2000
Externally publishedYes

Fingerprint

Bungarus
disulfides
Disulfides
acetylcholine
Fingers
Acetylcholine
Molecules
Aptitude
R Factors
Neurotoxins
tracing
Least-Squares Analysis
Carrier concentration
amino acids
molecules
Crystal structure
X-Rays
Electrons
Amino Acids
X rays

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods. / Kuhn, P.; Deacon, A. M.; Comoso, S.; Rajaseger, G.; Kini, R. M.; Uson, I.; Kolatkar, Prasanna.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 56, No. 11, 29.11.2000, p. 1401-1407.

Research output: Contribution to journalArticle

@article{14a609457ccd4a7d91f53c544af594dc,
title = "The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods",
abstract = "Bucandin is a novel presynaptic neurotoxin isolated from Bungarus candidus (Malayan krait). It has the unique property of enhancing presynaptic acetylcholine release and represents a family of three-finger toxins with an additional disulfide in the first loop. There are no existing structures from this sub-category of three-finger toxins. The X-ray crystal structure of bucandin has been determined by the Shake-and-Bake direct-methods procedure. The resulting electron-density maps were of outstanding quality and allowed the automated tracing of 61 of the 63 amino-acid residues, including their side chains, and the placement of 48 solvent molecules. The 0.97 {\AA} resolution full-matrix least-squares refinement converged to a crystallographic R factor of 12.4{\%} and the final model contains 118 solvent molecules. This is the highest resolution structure of any member of the three-finger toxin family and thus it can serve as the best model for other members of the family. Furthermore, the structure of this novel toxin will help in understanding its unique ability to enhance acetylcholine release. The unique structure resulting from the fifth disulfide bond residing in the first loop improves the understanding of other toxins with a similar arrangement of disulfide bonds.",
author = "P. Kuhn and Deacon, {A. M.} and S. Comoso and G. Rajaseger and Kini, {R. M.} and I. Uson and Prasanna Kolatkar",
year = "2000",
month = "11",
day = "29",
doi = "10.1107/S0907444900011501",
language = "English",
volume = "56",
pages = "1401--1407",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

TY - JOUR

T1 - The atomic resolution structure of bucandin, a novel toxin isolated from the Malayan krait, determined by direct methods

AU - Kuhn, P.

AU - Deacon, A. M.

AU - Comoso, S.

AU - Rajaseger, G.

AU - Kini, R. M.

AU - Uson, I.

AU - Kolatkar, Prasanna

PY - 2000/11/29

Y1 - 2000/11/29

N2 - Bucandin is a novel presynaptic neurotoxin isolated from Bungarus candidus (Malayan krait). It has the unique property of enhancing presynaptic acetylcholine release and represents a family of three-finger toxins with an additional disulfide in the first loop. There are no existing structures from this sub-category of three-finger toxins. The X-ray crystal structure of bucandin has been determined by the Shake-and-Bake direct-methods procedure. The resulting electron-density maps were of outstanding quality and allowed the automated tracing of 61 of the 63 amino-acid residues, including their side chains, and the placement of 48 solvent molecules. The 0.97 Å resolution full-matrix least-squares refinement converged to a crystallographic R factor of 12.4% and the final model contains 118 solvent molecules. This is the highest resolution structure of any member of the three-finger toxin family and thus it can serve as the best model for other members of the family. Furthermore, the structure of this novel toxin will help in understanding its unique ability to enhance acetylcholine release. The unique structure resulting from the fifth disulfide bond residing in the first loop improves the understanding of other toxins with a similar arrangement of disulfide bonds.

AB - Bucandin is a novel presynaptic neurotoxin isolated from Bungarus candidus (Malayan krait). It has the unique property of enhancing presynaptic acetylcholine release and represents a family of three-finger toxins with an additional disulfide in the first loop. There are no existing structures from this sub-category of three-finger toxins. The X-ray crystal structure of bucandin has been determined by the Shake-and-Bake direct-methods procedure. The resulting electron-density maps were of outstanding quality and allowed the automated tracing of 61 of the 63 amino-acid residues, including their side chains, and the placement of 48 solvent molecules. The 0.97 Å resolution full-matrix least-squares refinement converged to a crystallographic R factor of 12.4% and the final model contains 118 solvent molecules. This is the highest resolution structure of any member of the three-finger toxin family and thus it can serve as the best model for other members of the family. Furthermore, the structure of this novel toxin will help in understanding its unique ability to enhance acetylcholine release. The unique structure resulting from the fifth disulfide bond residing in the first loop improves the understanding of other toxins with a similar arrangement of disulfide bonds.

UR - http://www.scopus.com/inward/record.url?scp=0033732304&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033732304&partnerID=8YFLogxK

U2 - 10.1107/S0907444900011501

DO - 10.1107/S0907444900011501

M3 - Article

VL - 56

SP - 1401

EP - 1407

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 11

ER -