1tdj

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{{Seed}}
 
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[[Image:1tdj.png|left|200px]]
 
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==THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_1tdj", creates the "Structure Box" on the page.
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<StructureSection load='1tdj' size='340' side='right'caption='[[1tdj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tdj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TDJ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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{{STRUCTURE_1tdj| PDB=1tdj | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdj OCA], [https://pdbe.org/1tdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tdj RCSB], [https://www.ebi.ac.uk/pdbsum/1tdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tdj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ILVA_ECOLI ILVA_ECOLI] Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.<ref>PMID:13405870</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/td/1tdj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tdj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI===
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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<ref>PMID:9562556</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tdj" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9562556}}, adds the Publication Abstract to the page
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9562556 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9562556}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TDJ 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=1TDJ OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9562556 9562556]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Threonine ammonia-lyase]]
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[[Category: Eisenstein E]]
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[[Category: Eisenstein, E.]]
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[[Category: Gallagher DT]]
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[[Category: Gallagher, D T.]]
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[[Category: Gilliland GL]]
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[[Category: Gilliland, G L.]]
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[[Category: Xiao G]]
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[[Category: Xiao, G.]]
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[[Category: Allostery]]
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[[Category: Cooperative]]
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[[Category: Isoleucine biosynthesis]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Regulation]]
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[[Category: Tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:15:22 2008''
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Current revision

THREONINE DEAMINASE (BIOSYNTHETIC) FROM E. COLI

PDB ID 1tdj

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