1xcf: Difference between revisions

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[[Image:1xcf.jpg|left|200px]]<br /><applet load="1xcf" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1xcf.jpg|left|200px]]
caption="1xcf, resolution 1.8&Aring;" />
 
'''Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli'''<br />
{{Structure
|PDB= 1xcf |SIZE=350|CAPTION= <scene name='initialview01'>1xcf</scene>, resolution 1.8&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20]
|GENE=
}}
 
'''Crystal structure of P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1XCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCF OCA].  
1XCF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCF OCA].  


==Reference==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15451433 15451433]
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]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Tryptophan synthase]]
[[Category: Tryptophan synthase]]
[[Category: Jang, S B.]]
[[Category: Jang, S B.]]
[[Category: a-subunits]]
[[Category: a-subunit]]
[[Category: e coli]]
[[Category: e coli]]
[[Category: p28l/y173f double mutants]]
[[Category: p28l/y173f double mutant]]
[[Category: tryptophan synthase]]
[[Category: tryptophan synthase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:22 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:57 2008''

Revision as of 16:07, 20 March 2008

File:1xcf.jpg


PDB ID 1xcf

Drag the structure with the mouse to rotate
, resolution 1.8Å
Activity: Tryptophan synthase, with EC number 4.2.1.20
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

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

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