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[[Image:1f61.gif|left|200px]]<br /><applet load="1f61" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f61, resolution 2.00&Aring;" />
'''CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS==
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.
<StructureSection load='1f61' size='340' side='right'caption='[[1f61]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1F61 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 <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F61 OCA].  
</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>
 
<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>
==Reference==
<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>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10932251 10932251]
</table>
[[Category: Isocitrate lyase]]
== Function ==
[[Category: Mycobacterium tuberculosis]]
[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).
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Bentrup, K H.Hoener zu.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Jr., W R.Jacobs.]]
Check<jmol>
[[Category: McKinney, J D.]]
  <jmolCheckbox>
[[Category: Russell, D G.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f61_consurf.spt"</scriptWhenChecked>
[[Category: Sacchettini, J C.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Sharma, S.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Sharma, V.]]
  </jmolCheckbox>
[[Category: TBSGC, TB Structural Genomics Consortium.]]
</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].
[[Category: MG]]
<div style="clear:both"></div>
[[Category: alpha-beta barrel]]
__TOC__
[[Category: apo-enzyme]]
</StructureSection>
[[Category: open conformation]]
[[Category: Large Structures]]
[[Category: protein structure initiative]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: psi]]
[[Category: Hoener zu Bentrup KH]]
[[Category: structural genomics]]
[[Category: Jacobs Jr WR]]
[[Category: swapped helices]]
[[Category: McKinney JD]]
[[Category: tb structural genomics consortium]]
[[Category: Russell DG]]
[[Category: tbsgc]]
[[Category: Sacchettini JC]]
 
[[Category: Sharma S]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:16 2008''
[[Category: Sharma V]]

Latest revision as of 07:11, 7 February 2024

CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS

1f61, resolution 2.00Å

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