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1wat
From Proteopedia
(New page: 200px<br /><applet load="1wat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wat, resolution 3.0Å" /> '''THE THREE-DIMENSIONAL...) |
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| - | [[Image:1wat.gif|left|200px]]<br /><applet load="1wat" size=" | + | [[Image:1wat.gif|left|200px]]<br /><applet load="1wat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wat, resolution 3.0Å" /> | caption="1wat, resolution 3.0Å" /> | ||
'''THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR'''<br /> | '''THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of the ligand-binding domain of the | + | The three-dimensional structures of the ligand-binding domain of the wild-type Salmonella typhimurium aspartate receptor have been determined in the absence (apo) and presence of bound aspartate (complex) and compared to a cross-linked mutant containing a cysteine at position 36 which does not change signaling behavior of the intact receptor. The structures of the wild-type forms were determined in order to assess the effects of cross-linking on the structure and its influence on conformational changes upon ligand binding. As in the case of the cross-linked mutant receptor, the non-cross-linked ligand-binding domain is dimeric and is composed of 4-alpha-helical bundle monomer subunits related by a crystallographic 2-fold axis in the unbound form and by a non-crystallographic axis in the aspartate-bound form. A comparative study between the non-cross-linked and cross-linked structures has led to the following observations: 1) The long N-terminal helices of the individual subunits in the cross-linked structures are bent toward each other to accommodate the disulfide bond. 2) The rest of the subunit conformation is very similar to that of the wild-type. 3) The intersubunit angle of the cross-linked apo structure is larger by about 13 degrees when compared to the wild-type apo structure. 4) The nature and magnitude of the aspartate-induced conformational changes in the non-cross-linked wild-type structures are very similar to those of the cross-linked structures. |
==About this Structure== | ==About this Structure== | ||
| - | 1WAT 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 ASP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WAT 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=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAT OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kim, S | + | [[Category: Kim, S H.]] |
[[Category: ASP]] | [[Category: ASP]] | ||
[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:15 2008'' |
Revision as of 13:42, 21 February 2008
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THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR
Overview
The three-dimensional structures of the ligand-binding domain of the wild-type Salmonella typhimurium aspartate receptor have been determined in the absence (apo) and presence of bound aspartate (complex) and compared to a cross-linked mutant containing a cysteine at position 36 which does not change signaling behavior of the intact receptor. The structures of the wild-type forms were determined in order to assess the effects of cross-linking on the structure and its influence on conformational changes upon ligand binding. As in the case of the cross-linked mutant receptor, the non-cross-linked ligand-binding domain is dimeric and is composed of 4-alpha-helical bundle monomer subunits related by a crystallographic 2-fold axis in the unbound form and by a non-crystallographic axis in the aspartate-bound form. A comparative study between the non-cross-linked and cross-linked structures has led to the following observations: 1) The long N-terminal helices of the individual subunits in the cross-linked structures are bent toward each other to accommodate the disulfide bond. 2) The rest of the subunit conformation is very similar to that of the wild-type. 3) The intersubunit angle of the cross-linked apo structure is larger by about 13 degrees when compared to the wild-type apo structure. 4) The nature and magnitude of the aspartate-induced conformational changes in the non-cross-linked wild-type structures are very similar to those of the cross-linked structures.
About this Structure
1WAT is a Single protein structure of sequence from Salmonella typhimurium with as ligand. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding., Yeh JI, Biemann HP, Pandit J, Koshland DE, Kim SH, J Biol Chem. 1993 May 5;268(13):9787-92. PMID:8486661
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