1eci: Difference between revisions

Revision as of 00:29, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1eci.png

Template:STRUCTURE 1eci

ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)

Template:ABSTRACT PUBMED 7881269

About this StructureAbout this Structure

1ECI is a Protein complex structure of sequences from Ectatomma tuberculatum. Full experimental information is available from OCA.

ReferenceReference

Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom., Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS, J Biomol NMR. 1995 Jan;5(1):1-13. PMID:7881269

Page seeded by OCA on Tue Jul 1 00:29:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)'''
+===ECTATOMIN (WATER SOLUTION, NMR 20 STRUCTURES)===
-==Overview==
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-Two-dimensional 1H NMR techniques were used to determine the spatial structure of ectatomin, a toxin from the venom of the ant Ectatomma tuberculatum. Nearly complete proton resonance assignments for two chains of ectatomin (37 and 34 amino acid residues, respectively) were obtained using 2D TOCSY, DQF-COSY and NOESY experiments. The cross-peak volumes in NOESY spectra were used to define the local structure of the protein and generate accurate proton-proton distance constraints employing the MARDIGRAS program. Disulfide bonds were located by analyzing the global fold of ectatomin, calculated with the distance geometry program DIANA. These data, combined with data on the rate of exchange of amide protons with deuterium, were used to obtain a final set of 20 structures by DIANA. These structures were refined by unrestrained energy minimization using the CHARMm program. The resulting rms deviations over 20 structures (excluding the mobile N- and c-termini of each chain) are 0.75 A for backbone heavy atoms, and 1.25 A for all heavy atoms. The conformations of the two chains are similar. Each chain consists of two alpha-helices and a hinge region of four residues; this forms a hairpin structure which is stabilized by disulfide bridges. The hinge regions of the two chains are connected together by a third disulfide bridge. Thus, ectatomin forms a four-alpha-helical bundle structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_7881269}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7881269 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7881269}}
 ==About this Structure==
-ECI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECI OCA].
+ECI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Ectatomma_tuberculatum Ectatomma tuberculatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ECI OCA].
 ==Reference==
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 [[Category: Ant venom]]
 [[Category: Pore-forming toxin]]
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