1wat
From Proteopedia
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|PDB= 1wat |SIZE=350|CAPTION= <scene name='initialview01'>1wat</scene>, resolution 3.0Å | |PDB= 1wat |SIZE=350|CAPTION= <scene name='initialview01'>1wat</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene> | + | |LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wat OCA], [http://www.ebi.ac.uk/pdbsum/1wat PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wat RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kim, S H.]] | [[Category: Kim, S H.]] | ||
| - | [[Category: ASP]] | ||
[[Category: chemotaxis]] | [[Category: chemotaxis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:33:36 2008'' |
Revision as of 21:33, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 00:33:36 2008
