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New page: left|200px<br /><applet load="1k7x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k7x, resolution 1.70Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1k7x.jpg|left|200px]]<br /><applet load="1k7x" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1k7x.jpg|left|200px]]<br /><applet load="1k7x" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1k7x, resolution 1.70&Aring;" />
caption="1k7x, resolution 1.70&Aring;" />
'''CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN SYNTHASE'''<br />
'''CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN SYNTHASE'''<br />


==Overview==
==Overview==
The catalytic activity of the pyridoxal 5'-phosphate-dependent tryptophan, synthase alpha(2)beta(2) complex is allosterically regulated. The hydrogen, bond between the helix betaH6 residue betaSer(178) and the loop alphaL6, residue Gly(181) was shown to be critical in ligand-induced intersubunit, signaling, with the alpha-beta communication being completely lost in the, mutant betaSer(178) --&gt; Pro (Marabotti, A., De Biase, D., Tramonti, A., Bettati, S., and Mozzarelli, A. (2001) J. Biol. Chem. 276, 17747-17753)., The structural basis of the impaired allosteric regulation was, investigated by determining the crystal structures of the mutant, betaSer(178) --&gt; Pro in the absence and presence of the alpha-subunit, ligands indole-3-acetylglycine and glycerol 3-phosphate. The mutation, causes local and distant conformational changes especially in the, beta-subunit. The ligand-free structure exhibits larger differences at the, N-terminal part of helix betaH6, whereas the enzyme ligand complexes show, differences at the C-terminal side. In contrast to the wild-type enzyme, loop alphaL6 remains in an open conformation even in the presence of, alpha-ligands. This effects the equilibrium between active and inactive, conformations of the alpha-active site, altering k(cat) and K(m), and, forms the structural basis for the missing allosteric communication, between the alpha- and beta-subunits.
The catalytic activity of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is allosterically regulated. The hydrogen bond between the helix betaH6 residue betaSer(178) and the loop alphaL6 residue Gly(181) was shown to be critical in ligand-induced intersubunit signaling, with the alpha-beta communication being completely lost in the mutant betaSer(178) --&gt; Pro (Marabotti, A., De Biase, D., Tramonti, A., Bettati, S., and Mozzarelli, A. (2001) J. Biol. Chem. 276, 17747-17753). The structural basis of the impaired allosteric regulation was investigated by determining the crystal structures of the mutant betaSer(178) --&gt; Pro in the absence and presence of the alpha-subunit ligands indole-3-acetylglycine and glycerol 3-phosphate. The mutation causes local and distant conformational changes especially in the beta-subunit. The ligand-free structure exhibits larger differences at the N-terminal part of helix betaH6, whereas the enzyme ligand complexes show differences at the C-terminal side. In contrast to the wild-type enzyme loop alphaL6 remains in an open conformation even in the presence of alpha-ligands. This effects the equilibrium between active and inactive conformations of the alpha-active site, altering k(cat) and K(m), and forms the structural basis for the missing allosteric communication between the alpha- and beta-subunits.


==About this Structure==
==About this Structure==
1K7X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with NA and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K7X OCA].  
1K7X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1K7X OCA].  


==Reference==
==Reference==
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[[Category: tryptophan biosynthesis]]
[[Category: tryptophan biosynthesis]]


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