1qkd
From Proteopedia
(New page: 200px<br /><applet load="1qkd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qkd, resolution 1.49Å" /> '''ERABUTOXIN'''<br /> ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qkd.jpg|left|200px]]<br /><applet load="1qkd" size=" | + | [[Image:1qkd.jpg|left|200px]]<br /><applet load="1qkd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qkd, resolution 1.49Å" /> | caption="1qkd, resolution 1.49Å" /> | ||
'''ERABUTOXIN'''<br /> | '''ERABUTOXIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Erabutoxin a has been crystallized in its monomeric and dimeric forms. The | + | Erabutoxin a has been crystallized in its monomeric and dimeric forms. The structures were refined at 1.50 and 1.49 A resolution, respectively, using synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.84, b = 46.62, c = 21.22 A for the monomer and a = 55.32, b = 53.54, c = 40.76 A for the dimer. Using starting models from earlier structure determinations, the monomeric structure refined to an R value of 16.7% (8004 unique reflections, 17.0-1.50 A resolution range), while the dimeric structure has been solved by the molecular-replacement method with a final R value of 16.9% (19 444 unique reflections, 17.4-1.49 A resolution range). The high-resolution electron-density maps clearly revealed significant discrete disorder in the proteins and allowed an accurate determination of the solvent structure. For the monomer, the side chains of six residues were modelled with alternate conformers and 106 sites for water molecules and one site for a sulfate ion were included in the final model, whereas for the dimer, 206 sites for water molecules were included and both C-terminal residues together with the side chains of 11 residues adopted alternative conformations. A comparison was made with earlier structure determinations. The features of the solvent structure of the erabutoxin molecules are discussed in detail. |
==About this Structure== | ==About this Structure== | ||
| - | 1QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http:// | + | 1QKD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKD OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Laticauda semifasciata]] | [[Category: Laticauda semifasciata]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kanellopoulos, P | + | [[Category: Kanellopoulos, P N.]] |
[[Category: Nastopoulos, V.]] | [[Category: Nastopoulos, V.]] | ||
[[Category: Tsernoglou, D.]] | [[Category: Tsernoglou, D.]] | ||
| Line 19: | Line 19: | ||
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:35 2008'' |
Revision as of 12:40, 21 February 2008
|
ERABUTOXIN
Overview
Erabutoxin a has been crystallized in its monomeric and dimeric forms. The structures were refined at 1.50 and 1.49 A resolution, respectively, using synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.84, b = 46.62, c = 21.22 A for the monomer and a = 55.32, b = 53.54, c = 40.76 A for the dimer. Using starting models from earlier structure determinations, the monomeric structure refined to an R value of 16.7% (8004 unique reflections, 17.0-1.50 A resolution range), while the dimeric structure has been solved by the molecular-replacement method with a final R value of 16.9% (19 444 unique reflections, 17.4-1.49 A resolution range). The high-resolution electron-density maps clearly revealed significant discrete disorder in the proteins and allowed an accurate determination of the solvent structure. For the monomer, the side chains of six residues were modelled with alternate conformers and 106 sites for water molecules and one site for a sulfate ion were included in the final model, whereas for the dimer, 206 sites for water molecules were included and both C-terminal residues together with the side chains of 11 residues adopted alternative conformations. A comparison was made with earlier structure determinations. The features of the solvent structure of the erabutoxin molecules are discussed in detail.
About this Structure
1QKD is a Single protein structure of sequence from Laticauda semifasciata. Full crystallographic information is available from OCA.
Reference
Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution., Nastopoulos V, Kanellopoulos PN, Tsernoglou D, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):964-74. PMID:9757111
Page seeded by OCA on Thu Feb 21 14:40:35 2008
