1kfb: Difference between revisions

Revision as of 10:15, 2 July 2008

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File:1kfb.png

Template:STRUCTURE 1kfb

CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol PhosphateCRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate

Template:ABSTRACT PUBMED 12460570

About this StructureAbout this Structure

1KFB is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase., Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I, J Mol Biol. 2002 Dec 6;324(4):677-90. PMID:12460570

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

OCA

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-'''CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate'''
+===CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate===
-==Overview==
+<!--
-The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved alphaThr183 residue is part of loop alphaL6 and is located next to the alpha-active site and forms part of the alpha-beta subunit interface. The role of the interactions of alphaThr183 in alpha-site catalysis and allosteric regulation was investigated by analyzing the kinetics and crystal structures of the isosteric mutant alphaThr183Val. The mutant displays strongly impaired allosteric alpha-beta communication, and the catalytic activity of the alpha-reaction is reduced one hundred fold, whereas the beta-activity is not affected. The structural work establishes that the basis for the missing inter-subunit signaling is the lack of loop alphaL6 closure even in the presence of the alpha-subunit ligands, 3-indolyl-D-glycerol 3'-phosphate, or 3-indolylpropanol 3'-phosphate. The structural basis for the reduced alpha-activity has its origins in the missing hydrogen bond between alphaThr183 and the catalytic residue, alphaAsp60.
+The line below this paragraph, {{ABSTRACT_PUBMED_12460570}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12460570 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12460570}}
 ==About this Structure==
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 [[Category: Weyand, M.]]
 [[Category: Helix]]
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