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New page: left|200px<br /><applet load="1dqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dqu, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1dqu.jpg|left|200px]]<br /><applet load="1dqu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dqu, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE ISOCITRATE LYASE FROM ASPERGILLUS NIDULANS==
BACKGROUND: Isocitrate lyase catalyses the first committed step of the, carbon-conserving glyoxylate bypass, the Mg(2+)-dependent reversible, cleavage of isocitrate into succinate and glyoxylate. This metabolic, pathway is an inviting target for the control of a number of diseases, because the enzymes involved in this cycle have been identified in many, pathogens including Mycobacterium leprae and Leishmania. RESULTS: As part, of a programme of rational drug design the structure of the tetrameric, Aspergillus nidulans isocitrate lyase and its complex with glyoxylate and, a divalent cation have been solved to 2.8 A resolution using X-ray, diffraction. Each subunit comprises two domains, one of which adopts a, folding pattern highly reminiscent of the triose phosphate isomerase (TIM), barrel. A 'knot' between subunits observed in the three-dimensional, structure, involving residues towards the C terminus, implies that, tetramer assembly involves considerable flexibility in this part of the, protein. CONCLUSIONS: Difference Fourier analysis together with the, pattern of sequence conservation has led to the identification of both the, glyoxylate and metal binding sites and implicates the C-terminal end of, the TIM barrel as the active site, which is consistent with studies of, other enzymes with this fold. Two disordered regions of the polypeptide, chain lie close to the active site, one of which includes a critical, cysteine residue suggesting that conformational rearrangements are, essential for catalysis. Structural similarities between isocitrate lyase, and both PEP mutase and enzymes belonging to the enolase superfamily, suggest possible relationships in aspects of the mechanism.
<StructureSection load='1dqu' size='340' side='right'caption='[[1dqu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dqu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQU FirstGlance]. <br>
1DQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DQU 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]] 2.8&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqu OCA], [https://pdbe.org/1dqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqu RCSB], [https://www.ebi.ac.uk/pdbsum/1dqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqu ProSAT]</span></td></tr>
==Reference==
</table>
The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans., Britton K, Langridge S, Baker PJ, Weeradechapon K, Sedelnikova SE, De Lucas JR, Rice DW, Turner G, Structure. 2000 Apr 15;8(4):349-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10801489 10801489]
== Function ==
[[Category: Emericella nidulans]]
[https://www.uniprot.org/uniprot/ACEA_EMENI ACEA_EMENI]
[[Category: Isocitrate lyase]]
== Evolutionary Conservation ==
[[Category: Single protein]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Baker, P.J.]]
Check<jmol>
[[Category: Britton, K.L.]]
  <jmolCheckbox>
[[Category: Langridge, S.J.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqu_consurf.spt"</scriptWhenChecked>
[[Category: Lucas, J.R.De.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Rice, D.W.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Sedelnikova, S.E.]]
  </jmolCheckbox>
[[Category: Turner, G.]]
</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=1dqu ConSurf].
[[Category: Weeradechapon, K.]]
<div style="clear:both"></div>
[[Category: beta barrel]]
__TOC__
 
</StructureSection>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:30:19 2007''
[[Category: Aspergillus nidulans]]
[[Category: Large Structures]]
[[Category: Baker PJ]]
[[Category: Britton KL]]
[[Category: De Lucas JR]]
[[Category: Langridge SJ]]
[[Category: Rice DW]]
[[Category: Sedelnikova SE]]
[[Category: Turner G]]
[[Category: Weeradechapon K]]
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