1tdj

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[[Image:1tdj.jpg|left|200px]]
[[Image:1tdj.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1tdj |SIZE=350|CAPTION= <scene name='initialview01'>1tdj</scene>, resolution 2.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1tdj", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</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/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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1tdj| PDB=1tdj | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdj OCA], [http://www.ebi.ac.uk/pdbsum/1tdj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tdj RCSB]</span>
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}}
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'''THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI'''
'''THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI'''
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[[Category: Gilliland, G L.]]
[[Category: Gilliland, G L.]]
[[Category: Xiao, G.]]
[[Category: Xiao, G.]]
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[[Category: allostery]]
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[[Category: Allostery]]
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[[Category: cooperative]]
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[[Category: Cooperative]]
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[[Category: isoleucine biosynthesis]]
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[[Category: Isoleucine biosynthesis]]
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[[Category: pyridoxal phosphate]]
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[[Category: Pyridoxal phosphate]]
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[[Category: regulation]]
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[[Category: Regulation]]
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[[Category: tetramer]]
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[[Category: Tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:49:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:38 2008''
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Revision as of 06:49, 3 May 2008

Image:1tdj.jpg

Template:STRUCTURE 1tdj

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. 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 Page seeded by OCA on Sat May 3 09:49:28 2008

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