From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1wat.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1wat.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1wat| PDB=1wat | SCENE= }} | | {{STRUCTURE_1wat| PDB=1wat | SCENE= }} |
| | | | |
| - | '''THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8486661}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8486661 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8486661}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 24: |
Line 28: |
| | [[Category: Kim, S H.]] | | [[Category: Kim, S H.]] |
| | [[Category: Chemotaxis]] | | [[Category: Chemotaxis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:23:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:19:56 2008'' |
Revision as of 10:20, 29 July 2008
Template:STRUCTURE 1wat
THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR
Template:ABSTRACT PUBMED 8486661
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 Tue Jul 29 13:19:56 2008
