2lig
From Proteopedia
(New page: 200px<br /><applet load="2lig" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lig, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:2lig.jpg|left|200px]]<br /><applet load="2lig" size=" | + | [[Image:2lig.jpg|left|200px]]<br /><applet load="2lig" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2lig, resolution 2.0Å" /> | caption="2lig, resolution 2.0Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND'''<br /> | '''THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of an active, disulfide cross-linked dimer | + | The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling. |
==About this Structure== | ==About this Structure== | ||
| - | 2LIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with SO4, ASP and PHN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2LIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ASP:'>ASP</scene> and <scene name='pdbligand=PHN:'>PHN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LIG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Junior, D | + | [[Category: Junior, D E.Koshland.]] |
| - | [[Category: Kim, S | + | [[Category: Kim, S H.]] |
[[Category: Milburn, M.]] | [[Category: Milburn, M.]] | ||
| - | [[Category: Prive, G | + | [[Category: Prive, G G.]] |
[[Category: Scott, W.]] | [[Category: Scott, W.]] | ||
| - | [[Category: Yeh, J | + | [[Category: Yeh, J I.]] |
[[Category: ASP]] | [[Category: ASP]] | ||
[[Category: PHN]] | [[Category: PHN]] | ||
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[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:08 2008'' |
Revision as of 16:07, 21 February 2008
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THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND
Overview
The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.
About this Structure
2LIG is a Single protein structure of sequence from Salmonella typhimurium with , and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand., Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, Jancarik J, Koshland DE Jr, Kim SH, Science. 1991 Nov 29;254(5036):1342-7. PMID:1660187
Page seeded by OCA on Thu Feb 21 18:07:08 2008
Categories: Salmonella typhimurium | Single protein | Junior, D E.Koshland. | Kim, S H. | Milburn, M. | Prive, G G. | Scott, W. | Yeh, J I. | ASP | PHN | SO4 | Chemotaxis
