1g1b

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[[Image:1g1b.jpg|left|200px]]
 
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==CHORISMATE LYASE (WILD-TYPE) WITH BOUND PRODUCT==
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The line below this paragraph, containing "STRUCTURE_1g1b", creates the "Structure Box" on the page.
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<StructureSection load='1g1b' size='340' side='right'caption='[[1g1b]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1g1b]] is a 2 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=1G1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.99&#8491;</td></tr>
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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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{{STRUCTURE_1g1b| PDB=1g1b | SCENE= }}
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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=1g1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1b OCA], [https://pdbe.org/1g1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1b RCSB], [https://www.ebi.ac.uk/pdbsum/1g1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1b ProSAT]</span></td></tr>
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</table>
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'''CHORISMATE LYASE (WILD-TYPE) 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/g1/1g1b_consurf.spt"</scriptWhenChecked>
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1G1B 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=1G1B 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=1g1b 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 J.]]
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[[Category: Holden MJ]]
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[[Category: Howard, A.]]
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[[Category: Howard A]]
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[[Category: Kim, K J.]]
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[[Category: Kim KJ]]
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[[Category: Mayhew, M.]]
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[[Category: Mayhew M]]
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[[Category: Vilker, V L.]]
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[[Category: Vilker VL]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:00:30 2008''
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Current revision

CHORISMATE LYASE (WILD-TYPE) WITH BOUND PRODUCT

PDB ID 1g1b

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