View source for 2cfq


==Sugar Free Lactose Permease at neutral pH==
<StructureSection load='2cfq' size='340' side='right'caption='[[2cfq]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cfq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Lactose Permease|Lactose Permease]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Guan L]]
[[Category: Iwata S]]
[[Category: Kaback HR]]
[[Category: Mirza O]]
[[Category: Verner G]]