1v7y

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[[Image:1v7y.gif|left|200px]]
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{{Structure
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|PDB= 1v7y |SIZE=350|CAPTION= <scene name='initialview01'>1v7y</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1v7y", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1v7y| PDB=1v7y | SCENE= }}
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|RELATEDENTRY=[[1wq5|1WQ5]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7y OCA], [http://www.ebi.ac.uk/pdbsum/1v7y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v7y RCSB]</span>
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'''Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature'''
'''Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature'''
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[[Category: Tsukihara, T.]]
[[Category: Tsukihara, T.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: Rsgi]]
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[[Category: structural genomic]]
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[[Category: Structural genomic]]
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[[Category: tryptophan]]
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[[Category: Tryptophan]]
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[[Category: tryptophan synthase]]
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[[Category: Tryptophan synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:11:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:20:43 2008''
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Revision as of 09:11, 3 May 2008

Image:1v7y.gif

Template:STRUCTURE 1v7y

Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature


Overview

When the tryptophan synthase alpha- and beta(2)-subunits combine to form the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is stimulated by 1-2 orders of magnitude. To elucidate the structural basis of this mutual activation, it is necessary to determine the structures of the alpha- and beta-subunits alone and together with the alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase alpha(2)beta(2)-complex from Salmonella typhimurium (Stalpha(2)beta(2)-complex) have already been reported. However, the structures of the subunit alone from mesophiles have not yet been determined. The structure of the tryptophan synthase alpha-subunit alone from Escherichia coli (Ecalpha-subunit) was determined by an X-ray crystallographic analysis at 2.3 A, which is the first report on the subunits alone from the mesophiles. The biggest difference between the structures of the Ecalpha-subunit alone and the alpha-subunit in the Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in the Stalpha-subunit, including an active site residue (Asp60), was changed to a flexible loop in the Ecalpha-subunit alone. The conversion of the helix to a loop resulted in the collapse of the correct active site conformation. This region is also an important part for the mutual activation in the Stalpha(2)beta(2)-complex and interaction with the beta-subunit. These results suggest that the formation of helix 2'that is essential for the stimulation of the enzymatic activity of the alpha-subunit is constructed by the induced-fit mode involved in conformational changes upon interaction between the alpha- and beta-subunits. This also confirms the prediction of the conformational changes based on the thermodynamic analysis for the association between the alpha- and beta-subunits.

About this Structure

1V7Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone., Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K, Biochemistry. 2005 Feb 1;44(4):1184-92. PMID:15667212 Page seeded by OCA on Sat May 3 12:11:45 2008

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