Sandbox Reserved 1228
From Proteopedia
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== Subunits == | == Subunits == | ||
<b> Subunit A </b> | <b> Subunit A </b> | ||
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1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL | 1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL | ||
<b> Subunit B </b> | <b> Subunit B </b> | ||
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1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK | 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK | ||
Revision as of 19:20, 26 April 2017
Contents |
ECTATOMIN 1ECI
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Ectatomin is a water soluble toxic component from Ectatomma tuberculatum ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.
Structure
Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution.
Subunits
Subunit A
1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL
Subunit B
1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK
Function
A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half. When inserted into an artificial membrane, ectatomin forms an iron pore. The formation of the pore requires reorganization of its helices.
Spectroscopy
1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms.
References
Arseniev, A S, et al. "Toxic Principle of Selva Ant Venom Is a Pore-Forming Protein Transformer." FEBS Letters, vol. 347, no. 2-3, 27 June 1994, pp. 112-116. EBSCOhost, proxy.library.maryville.edu/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=mdc&AN=8033986&site=eds-live&scope=site.
Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS (January 1995). "Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom". J. Biomol. NMR. 5 (1): 1–13. doi:10.1007/BF00227465. PMID 7881269.
Pluzhnikov, Kirill, et al. “Analysis of Ectatomin Action on Cell Membranes.” European Journal of Biochemistry 262.2 (1999):501. Academic Search Complete. Web. 13 Feb. 2017
Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.
