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1f61
From Proteopedia
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| - | [[ | + | ==CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS== |
| + | <StructureSection load='1f61' size='340' side='right' caption='[[1f61]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1f61]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F61 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f61 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f61 RCSB], [http://www.ebi.ac.uk/pdbsum/1f61 PDBsum], [http://www.topsan.org/Proteins/TBSGC/1f61 TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f61_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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:10932251<ref>PMID:10932251</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
| - | < | + | |
[[Category: Isocitrate lyase]] | [[Category: Isocitrate lyase]] | ||
[[Category: Mycobacterium tuberculosis h37rv]] | [[Category: Mycobacterium tuberculosis h37rv]] | ||
| - | [[Category: Bentrup, K H.Hoener zu | + | [[Category: Bentrup, K H.Hoener zu]] |
| - | [[Category: Jacobs, W R | + | [[Category: Jacobs, W R]] |
| - | [[Category: McKinney, J D | + | [[Category: McKinney, J D]] |
| - | [[Category: Russell, D G | + | [[Category: Russell, D G]] |
| - | [[Category: Sacchettini, J C | + | [[Category: Sacchettini, J C]] |
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] |
| - | [[Category: Sharma, V | + | [[Category: Sharma, V]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
[[Category: Alpha-beta barrel]] | [[Category: Alpha-beta barrel]] | ||
[[Category: Apo-enzyme]] | [[Category: Apo-enzyme]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Open conformation]] | [[Category: Open conformation]] | ||
| - | [[Category: Protein structure initiative | + | [[Category: PSI, Protein structure initiative]] |
| - | + | ||
| - | + | ||
[[Category: Swapped helice]] | [[Category: Swapped helice]] | ||
| - | [[Category: Tb structural genomics consortium]] | ||
[[Category: Tbsgc]] | [[Category: Tbsgc]] | ||
Revision as of 18:51, 22 December 2014
CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS
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Categories: Isocitrate lyase | Mycobacterium tuberculosis h37rv | Bentrup, K H.Hoener zu | Jacobs, W R | McKinney, J D | Russell, D G | Sacchettini, J C | Sharma, S | Sharma, V | Structural genomic | Alpha-beta barrel | Apo-enzyme | Lyase | Open conformation | PSI, Protein structure initiative | Swapped helice | Tbsgc
