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1f61

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[[Image:1f61.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS==
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|PDB= 1f61 |SIZE=350|CAPTION= <scene name='initialview01'>1f61</scene>, resolution 2.00&Aring;
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<StructureSection load='1f61' size='340' side='right'caption='[[1f61]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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<table><tr><td colspan='2'>[[1f61]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F61 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Isocitrate_lyase Isocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.1 4.1.3.1]
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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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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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=1f61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f61 OCA], [https://pdbe.org/1f61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f61 RCSB], [https://www.ebi.ac.uk/pdbsum/1f61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f61 ProSAT], [https://www.topsan.org/Proteins/TBSGC/1f61 TOPSAN]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS'''
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== Function ==
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[https://www.uniprot.org/uniprot/ACEA_MYCTU ACEA_MYCTU] Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway (By similarity).
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Isocitrate lyase (ICL) plays a pivotal role in the persistence of Mycobacterium tuberculosis in mice by sustaining intracellular infection in inflammatory macrophages. The enzyme allows net carbon gain by diverting acetyl-CoA from beta-oxidation of fatty acids into the glyoxylate shunt pathway. Given its potential as a drug target against persistent infections, we solved its structure without ligand and in complex with two inhibitors. Covalent modification of an active site residue, Cys 191, by the inhibitor 3-bromopyruvate traps the enzyme in a catalytic conformation with the active site completely inaccessible to solvent. The structure of a C191S mutant of the enzyme with the inhibitor 3-nitropropionate provides further insight into the reaction mechanism.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f61_consurf.spt"</scriptWhenChecked>
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1F61 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F61 OCA].
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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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==Reference==
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</jmolCheckbox>
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Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis., Sharma V, Sharma S, Hoener zu Bentrup K, McKinney JD, Russell DG, Jacobs WR Jr, Sacchettini JC, Nat Struct Biol. 2000 Aug;7(8):663-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10932251 10932251]
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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=1f61 ConSurf].
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[[Category: Isocitrate lyase]]
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<div style="clear:both"></div>
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[[Category: Mycobacterium tuberculosis]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Bentrup, K H.Hoener zu.]]
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[[Category: Large Structures]]
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[[Category: Jr., W R.Jacobs.]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: McKinney, J D.]]
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[[Category: Hoener zu Bentrup KH]]
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[[Category: Russell, D G.]]
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[[Category: Jacobs Jr WR]]
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[[Category: Sacchettini, J C.]]
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[[Category: McKinney JD]]
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[[Category: Sharma, S.]]
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[[Category: Russell DG]]
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[[Category: Sharma, V.]]
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[[Category: Sacchettini JC]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
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[[Category: Sharma S]]
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[[Category: MG]]
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[[Category: Sharma V]]
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[[Category: alpha-beta barrel]]
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[[Category: apo-enzyme]]
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[[Category: open conformation]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomic]]
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[[Category: swapped helice]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:54 2008''
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Current revision

CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS

PDB ID 1f61

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