1enz

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(New page: 200px<br /><applet load="1enz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1enz, resolution 2.7&Aring;" /> '''CRYSTAL STRUCTURE AND...)
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[[Image:1enz.gif|left|200px]]<br /><applet load="1enz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1enz, resolution 2.7&Aring;" />
 
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'''CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS==
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Resistance to isoniazid in Mycobacterium tuberculosis can be mediated by, substitution of alanine for serine 94 in the InhA protein, the drug's, primary target. InhA was shown to catalyze the beta-nicotinamide adenine, dinucleotide (NADH)-specific reduction of 2-trans-enoyl-acyl carrier, protein, an essential step in fatty acid elongation. Kinetic analyses, suggested that isoniazid resistance is due to a decreased affinity of the, mutant protein for NADH. The three-dimensional structures of wild-type and, mutant InhA, refined to 2.2 and 2.7 angstroms, respectively, revealed that, drug resistance is directly related to a perturbation in the, hydrogen-bonding network that stabilizes NADH binding.
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<StructureSection load='1enz' size='340' side='right'caption='[[1enz]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1enz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ENZ FirstGlance]. <br>
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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]] 2.7&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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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=1enz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enz OCA], [https://pdbe.org/1enz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1enz RCSB], [https://www.ebi.ac.uk/pdbsum/1enz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1enz ProSAT], [https://www.topsan.org/Proteins/TBSGC/1enz TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/INHA_MYCTU INHA_MYCTU]
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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/en/1enz_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=1enz ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ENZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ENZ OCA].
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*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science. 1995 Mar 17;267(5204):1638-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7886450 7886450]
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[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Blanchard JS]]
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[[Category: Blanchard, J.S.]]
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[[Category: Dessen A]]
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[[Category: Dessen, A.]]
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[[Category: Jacobs Jr WR]]
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[[Category: Jr., W.R.Jacobs.]]
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[[Category: Quemard A]]
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[[Category: Quemard, A.]]
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[[Category: Sacchettini JC]]
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[[Category: Sacchettini, J.C.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: NAD]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:09:55 2007''
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Current revision

CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS

PDB ID 1enz

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