1wat: Difference between revisions

Revision as of 13:20, 29 July 2008

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File:1wat.png

Template:STRUCTURE 1wat

THE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTORTHE THREE-DIMENSIONAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF A WILD-TYPE BACTERIAL CHEMOTAXIS RECEPTOR

Template:ABSTRACT PUBMED 8486661

About this StructureAbout this Structure

1WAT is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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.
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+{{ABSTRACT_PUBMED_8486661}}
 ==About this Structure==
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 [[Category: Kim, S H.]]
 [[Category: Chemotaxis]]
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