3dtf

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[[Image:3dtf.png|left|200px]]
 
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==Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design==
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The line below this paragraph, containing "STRUCTURE_3dtf", creates the "Structure Box" on the page.
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<StructureSection load='3dtf' size='340' side='right'caption='[[3dtf]], [[Resolution|resolution]] 2.20&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'>[[3dtf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DTF 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]] 2.2&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3dtf| PDB=3dtf | 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=3dtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dtf OCA], [https://pdbe.org/3dtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dtf RCSB], [https://www.ebi.ac.uk/pdbsum/3dtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dtf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ILVE_MYCS2 ILVE_MYCS2] Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.<ref>PMID:20445230</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/dt/3dtf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3dtf 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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The branched-chain aminotransferase (BCAT) of Mycobacterium tuberculosis has been characterized as being essential to the survival of the bacterium. The enzyme is pyridoxal 5'-phosphate-dependent and belongs to the aminotransferase IIIa subfamily, to which the human BCATs also belong. The overall sequence similarity is high within the subfamily and the sequence identity among the active-site residues is high. In order to identify structurally unique features of M. tuberculosis BCAT, X-ray structural and functional analyses of the closely related BCAT from M. smegmatis were carried out. The crystal structures include the apo form at 2.2 A resolution and a 1.9 A structure of the holo form cocrystallized with the inhibitor O-benzylhydroxylamine (Obe). The analyses highlighted the active-site residues Tyr209 and Gly243 as being structurally unique characteristics of the mycobacterial BCATs relative to the human BCATs. The inhibitory activities of Obe and ammonium sulfate were verified in an inhibition assay. Modelling of the inhibitor Obe in the substrate pocket indicated potential for the design of a mycobacterial-specific inhibitor.
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===Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design===
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Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design.,Castell A, Mille C, Unge T Acta Crystallogr D Biol Crystallogr. 2010 May;66(Pt 5):549-57. Epub 2010 Apr 21. PMID:20445230<ref>PMID:20445230</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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The line below this paragraph, {{ABSTRACT_PUBMED_20445230}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3dtf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20445230 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20445230}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3dtf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DTF OCA].
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Castell A]]
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==Reference==
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[[Category: Unge T]]
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<ref group="xtra">PMID:020445230</ref><references group="xtra"/>
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[[Category: Branched-chain-amino-acid transaminase]]
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[[Category: Mycobacterium smegmatis]]
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[[Category: Castell, A.]]
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[[Category: Unge, T.]]
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[[Category: Aminotransferase]]
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[[Category: Open twisted alpha/beta]]
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[[Category: Transferase]]
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Current revision

Structural analysis of mycobacterial branched chain aminotransferase- implications for inhibitor design

PDB ID 3dtf

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