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1fw9

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[[Image:1fw9.jpg|left|200px]]
 
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{{Structure
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==CHORISMATE LYASE WITH BOUND PRODUCT==
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|PDB= 1fw9 |SIZE=350|CAPTION= <scene name='initialview01'>1fw9</scene>, resolution 1.40&Aring;
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<StructureSection load='1fw9' size='340' side='right'caption='[[1fw9]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PHB:P-HYDROXYBENZOIC ACID'>PHB</scene>
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<table><tr><td colspan='2'>[[1fw9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FW9 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.4&#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=PHB:P-HYDROXYBENZOIC+ACID'>PHB</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=1fw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw9 OCA], [https://pdbe.org/1fw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fw9 RCSB], [https://www.ebi.ac.uk/pdbsum/1fw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fw9 ProSAT]</span></td></tr>
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</table>
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'''CHORISMATE LYASE WITH BOUND PRODUCT'''
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== Function ==
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[https://www.uniprot.org/uniprot/UBIC_ECOLI UBIC_ECOLI] Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.[HAMAP-Rule:MF_01632]
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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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The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway. In Escherichia coli, CL is monomeric, with 164 residues. We have determined the structure of the CL product complex by crystallographic heavy-atom methods and report the structure at 1.4-A resolution for a fully active double Cys-to-Ser mutant and at 2.0-A resolution for the wild-type. The fold involves a 6-stranded antiparallel beta-sheet with no spanning helices and novel connectivity. The product is bound internally, adjacent to the sheet, with its polar groups coordinated by two main-chain amides and by the buried side-chains of Arg 76 and Glu 155. The 4HB is completely sequestered from solvent in a largely hydrophobic environment behind two helix-turn-helix loops. The extensive product binding that is observed is consistent with biochemical measurements of slow product release and 10-fold stronger binding of product than substrate. Substrate binding and kinetically rate-limiting product release apparently require the rearrangement of these active-site-covering loops. Implications for the biological function of the high product binding are considered in light of the unique cellular role of 4HB, which is produced by cytoplasmic CL but is used by the membrane-bound enzyme 4HB octaprenyltransferase.
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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/fw/1fw9_consurf.spt"</scriptWhenChecked>
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1FW9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW9 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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The crystal structure of chorismate lyase shows a new fold and a tightly retained product., Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL, Proteins. 2001 Aug 15;44(3):304-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11455603 11455603]
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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=1fw9 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gallagher, D T.]]
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[[Category: Gallagher DT]]
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[[Category: Holden, M.]]
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[[Category: Holden M]]
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[[Category: Howard, A.]]
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[[Category: Howard A]]
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[[Category: Mayhew, M.]]
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[[Category: Mayhew M]]
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[[Category: Vilker, V.]]
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[[Category: Vilker V]]
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[[Category: PHB]]
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[[Category: 123654 antiparallel sheet topology]]
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[[Category: new fold]]
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[[Category: ubiquinone pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:48 2008''
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Current revision

CHORISMATE LYASE WITH BOUND PRODUCT

PDB ID 1fw9

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