1r6j: Difference between revisions
New page: left|200px<br /> <applet load="1r6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6j, resolution 0.73Å" /> '''Ultrahigh resolutio... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1r6j.gif|left|200px]]<br /> | [[Image:1r6j.gif|left|200px]]<br /><applet load="1r6j" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1r6j" size=" | |||
caption="1r6j, resolution 0.73Å" /> | caption="1r6j, resolution 0.73Å" /> | ||
'''Ultrahigh resolution Crystal Structure of syntenin PDZ2'''<br /> | '''Ultrahigh resolution Crystal Structure of syntenin PDZ2'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the second PDZ domain of the scaffolding protein | The crystal structure of the second PDZ domain of the scaffolding protein syntenin was solved using data extending to 0.73 A resolution. The crystallographic model, including the hydrogen atoms and the anisotropic displacement parameters, was refined to a conventional R-factor of 7.5% and Rfree of 8.7%, making it the most precise crystallographic model of a protein molecule to date. The model reveals discrete disorder in several places in the molecule, and significant plasticity of the peptide bond, with some omega angles deviating by nearly 20 degrees from planarity. Most hydrogen atoms are easily identifiable in the electron density and weak hydrogen bonds of the C-H...O type are clearly visible between the beta-strands. The study sets a new standard for high-resolution protein crystallography. | ||
==About this Structure== | ==About this Structure== | ||
1R6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1R6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6J OCA]. | ||
==Reference== | ==Reference== | ||
| Line 15: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
[[Category: Derewenda, Z | [[Category: Derewenda, Z S.]] | ||
[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Kang, B | [[Category: Kang, B S.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: pdz]] | [[Category: pdz]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:37 2008'' | ||
Revision as of 15:47, 21 February 2008
|
Ultrahigh resolution Crystal Structure of syntenin PDZ2
OverviewOverview
The crystal structure of the second PDZ domain of the scaffolding protein syntenin was solved using data extending to 0.73 A resolution. The crystallographic model, including the hydrogen atoms and the anisotropic displacement parameters, was refined to a conventional R-factor of 7.5% and Rfree of 8.7%, making it the most precise crystallographic model of a protein molecule to date. The model reveals discrete disorder in several places in the molecule, and significant plasticity of the peptide bond, with some omega angles deviating by nearly 20 degrees from planarity. Most hydrogen atoms are easily identifiable in the electron density and weak hydrogen bonds of the C-H...O type are clearly visible between the beta-strands. The study sets a new standard for high-resolution protein crystallography.
About this StructureAbout this Structure
1R6J is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap between macromolecular and small molecule crystallography., Kang BS, Devedjiev Y, Derewenda U, Derewenda ZS, J Mol Biol. 2004 Apr 30;338(3):483-93. PMID:15081807
Page seeded by OCA on Thu Feb 21 14:47:37 2008