1xcf: Difference between revisions

Revision as of 00:41, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xcf.png

Template:STRUCTURE 1xcf

Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coliCrystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli

Template:ABSTRACT PUBMED 15451433

About this StructureAbout this Structure

1XCF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli., Jeong MS, Jeong JK, Lim WK, Jang SB, Biochem Biophys Res Commun. 2004 Oct 29;323(4):1257-64. PMID:15451433

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 P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli'''
+===Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli===
-==Overview==
+<!--
-The alpha-subunit of tryptophan synthase (alphaTS) catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is used to yield the amino acid tryptophan in tryptophan biosynthesis. Here, we report the first crystal structures of wild-type and double-mutant P28L/Y173F alpha-subunit of tryptophan synthase from Escherichia coli at 2.8 and 1.8A resolution, respectively. The structure of wild-type alphaTS from E. coli was similar to that of the alpha(2)beta(2) complex structure from Salmonella typhimurium. As compared with both structures, the conformational changes are mostly in the interface of alpha- and beta-subunits, and the substrate binding region. Two sulfate ions and two glycerol molecules per asymmetric unit bind with the residues in the active sites of the wild-type structure. Contrarily, double-mutant P28L/Y173F structure is highly closed at the window for the substrate binding by the conformational changes. The P28L substitution induces the exposure of hydrophobic amino acids and decreases the secondary structure that causes the aggregation. The Y173F suppresses to transfer a signal from the alpha-subunit core to the alpha-subunit surface involved in interactions with the beta-subunit and increases structural stability.
+The line below this paragraph, {{ABSTRACT_PUBMED_15451433}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15451433}}
 ==About this Structure==
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 ==Reference==
 Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli., Jeong MS, Jeong JK, Lim WK, Jang SB, Biochem Biophys Res Commun. 2004 Oct 29;323(4):1257-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15451433 15451433]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/12460570 12460570]
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
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 [[Category: P28l/y173f double mutant]]
 [[Category: Tryptophan synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:51:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:41:09 2008''