1tdj
From Proteopedia
(New page: 200px<br /><applet load="1tdj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tdj, resolution 2.8Å" /> '''THREONINE DEAMINASE (...) |
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| - | [[Image:1tdj.jpg|left|200px]]<br /><applet load="1tdj" size=" | + | [[Image:1tdj.jpg|left|200px]]<br /><applet load="1tdj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tdj, resolution 2.8Å" /> | caption="1tdj, resolution 2.8Å" /> | ||
'''THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI'''<br /> | '''THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Feedback inhibition of biosynthetic threonine deaminase (TD) | + | BACKGROUND: Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms. RESULTS: We report the crystal structure of TD at 2.8 A resolution. The tetramer has 222 symmetry, with C-terminal regulatory domains projecting out from a core of catalytic PLP-containing N-terminal domains. The subunits, and especially the regulatory domains, associate extensively to form dimers, which associate less extensively to form the tetramer. Within the dimer, each monomer twists approximately 150 degrees around a thin neck between the domains to place its catalytic domain adjacent to the regulatory domain of the other subunit. CONCLUSIONS: The structure of TD and its comparison with related structures and other data lead to the tentative identification of the regulatory binding site and revealed several implications for the allosteric mechanism. This work prepares the way for detailed structure/function studies of the complex allosteric behaviour of this enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1TDJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Threonine_ammonia-lyase Threonine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.19 4.3.1.19] Full crystallographic information is available from [http:// | + | 1TDJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Threonine_ammonia-lyase Threonine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.19 4.3.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Threonine ammonia-lyase]] | [[Category: Threonine ammonia-lyase]] | ||
[[Category: Eisenstein, E.]] | [[Category: Eisenstein, E.]] | ||
| - | [[Category: Gallagher, D | + | [[Category: Gallagher, D T.]] |
| - | [[Category: Gilliland, G | + | [[Category: Gilliland, G L.]] |
[[Category: Xiao, G.]] | [[Category: Xiao, G.]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:27 2008'' |
Revision as of 13:12, 21 February 2008
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THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI
Overview
BACKGROUND: Feedback inhibition of biosynthetic threonine deaminase (TD) from Escherichia coli provided one of the earliest examples of protein-based metabolic regulation. Isoleucine, the pathway end-product, and valine, the product of a parallel pathway, serve as allosteric inhibitor and activator, respectively. This enzyme is thus a useful model system for studying the structural basis of allosteric control mechanisms. RESULTS: We report the crystal structure of TD at 2.8 A resolution. The tetramer has 222 symmetry, with C-terminal regulatory domains projecting out from a core of catalytic PLP-containing N-terminal domains. The subunits, and especially the regulatory domains, associate extensively to form dimers, which associate less extensively to form the tetramer. Within the dimer, each monomer twists approximately 150 degrees around a thin neck between the domains to place its catalytic domain adjacent to the regulatory domain of the other subunit. CONCLUSIONS: The structure of TD and its comparison with related structures and other data lead to the tentative identification of the regulatory binding site and revealed several implications for the allosteric mechanism. This work prepares the way for detailed structure/function studies of the complex allosteric behaviour of this enzyme.
About this Structure
1TDJ is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Threonine ammonia-lyase, with EC number 4.3.1.19 Full crystallographic information is available from OCA.
Reference
Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase., Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein E, Structure. 1998 Apr 15;6(4):465-75. PMID:9562556
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