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2cfq

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[[Image:2cfq.gif|left|200px]]<br />
 
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<applet load="2cfq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cfq, resolution 2.95&Aring;" />
 
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'''SUGAR FREE LACTOSE PERMEASE AT NEUTRAL PH'''<br />
 
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==Overview==
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==Sugar Free Lactose Permease at neutral pH==
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Cation-coupled active transport is an essential cellular process found, ubiquitously in all living organisms. Here, we present two novel, ligand-free X-ray structures of the lactose permease (LacY) of Escherichia, coli determined at acidic and neutral pH, and propose a model for the, mechanism of coupling between lactose and H+ translocation. No, sugar-binding site is observed in the absence of ligand, and deprotonation, of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the, initial step in H+ transduction.
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<StructureSection load='2cfq' size='340' side='right'caption='[[2cfq]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cfq]] 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=2CFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CFQ FirstGlance]. <br>
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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]] 2.95&#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=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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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=2cfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfq OCA], [https://pdbe.org/2cfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cfq RCSB], [https://www.ebi.ac.uk/pdbsum/2cfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cfq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LACY_ECOLI LACY_ECOLI] Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cfq_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=2cfq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.
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==About this Structure==
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Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY.,Mirza O, Guan L, Verner G, Iwata S, Kaback HR EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:16525509<ref>PMID:16525509</ref>
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2CFQ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with HG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFQ OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY., Mirza O, Guan L, Verner G, Iwata S, Kaback HR, EMBO J. 2006 Mar 22;25(6):1177-83. Epub 2006 Mar 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16525509 16525509]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2cfq" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Guan, L.]]
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[[Category: Iwata, S.]]
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[[Category: Kaback, H.R.]]
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[[Category: Mirza, O.]]
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[[Category: Verner, G.]]
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[[Category: HG]]
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[[Category: formylation]]
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[[Category: lactose permease]]
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[[Category: lactose/h+ symport]]
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[[Category: sugar transport]]
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[[Category: transmembrane]]
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[[Category: transport mechanism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:36:16 2007''
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==See Also==
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*[[Lactose Permease|Lactose Permease]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Guan L]]
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[[Category: Iwata S]]
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[[Category: Kaback HR]]
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[[Category: Mirza O]]
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[[Category: Verner G]]

Current revision

Sugar Free Lactose Permease at neutral pH

PDB ID 2cfq

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