2sh1
From Proteopedia
(New page: 200px<br /><applet load="2sh1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2sh1" /> '''SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE ...) |
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'''SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY'''<br /> | '''SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the sea anemone polypeptide | + | The three-dimensional structure of the sea anemone polypeptide Stichodactyla helianthus neurotoxin I in aqueous solution has been determined using distance geometry and restrained molecular dynamics simulations based on NMR data acquired at 500 MHz. A set of 470 nuclear Overhauser enhancement values was measured, of which 216 were used as distance restraints in the structure determination along with 15 dihedral angles derived from coupling constants. After restrained molecular dynamics refinement, the eight structures that best fit the input data form a closely related family. They describe a structure that consists of a core of twisted, four-stranded, antiparallel beta-sheet encompassing residues 1-3, 19-24, 29-34, and 40-47, joined by three loops, two of which are well defined by the NMR data. The third loop, encompassing residues 7-16, is poorly defined by the data and is assumed to undergo conformational averaging in solution. Pairwise root mean square displacement values for the backbone heavy atoms of the eight best structures are 1.3 +/- 0.2A when the poorly defined loop is excluded and 3.6 +/- 1.0A for all backbone atoms. Refinement using restrained molecular dynamics improved the quality of the structures generated by distance geometry calculations with respect to the number of nuclear Overhauser enhancements violated, the size of the total distance violations and the total potential energies of the structures. The family of structures for S. heliathus neurotoxin I is compared with structures of related sea anemone proteins that also bind to the voltage-gated sodium channel. |
==About this Structure== | ==About this Structure== | ||
| - | 2SH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full crystallographic information is available from [http:// | + | 2SH1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SH1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Stichodactyla helianthus]] | [[Category: Stichodactyla helianthus]] | ||
| - | [[Category: Fogh, R | + | [[Category: Fogh, R H.]] |
| - | [[Category: Norton, R | + | [[Category: Norton, R S.]] |
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:09 2008'' |
Revision as of 16:49, 21 February 2008
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SOLUTION STRUCTURE OF NEUROTOXIN I FROM THE SEA ANEMONE STICHODACTYLA HELIANTHUS. A NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS STUDY
Overview
The three-dimensional structure of the sea anemone polypeptide Stichodactyla helianthus neurotoxin I in aqueous solution has been determined using distance geometry and restrained molecular dynamics simulations based on NMR data acquired at 500 MHz. A set of 470 nuclear Overhauser enhancement values was measured, of which 216 were used as distance restraints in the structure determination along with 15 dihedral angles derived from coupling constants. After restrained molecular dynamics refinement, the eight structures that best fit the input data form a closely related family. They describe a structure that consists of a core of twisted, four-stranded, antiparallel beta-sheet encompassing residues 1-3, 19-24, 29-34, and 40-47, joined by three loops, two of which are well defined by the NMR data. The third loop, encompassing residues 7-16, is poorly defined by the data and is assumed to undergo conformational averaging in solution. Pairwise root mean square displacement values for the backbone heavy atoms of the eight best structures are 1.3 +/- 0.2A when the poorly defined loop is excluded and 3.6 +/- 1.0A for all backbone atoms. Refinement using restrained molecular dynamics improved the quality of the structures generated by distance geometry calculations with respect to the number of nuclear Overhauser enhancements violated, the size of the total distance violations and the total potential energies of the structures. The family of structures for S. heliathus neurotoxin I is compared with structures of related sea anemone proteins that also bind to the voltage-gated sodium channel.
About this Structure
2SH1 is a Single protein structure of sequence from Stichodactyla helianthus. Full crystallographic information is available from OCA.
Reference
Solution structure of neurotoxin I from the sea anemone Stichodactyla helianthus. A nuclear magnetic resonance, distance geometry, and restrained molecular dynamics study., Fogh RH, Kem WR, Norton RS, J Biol Chem. 1990 Aug 5;265(22):13016-28. PMID:1973932
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