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[[Image:2v8n.jpg|left|200px]]
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{{STRUCTURE_2v8n|  PDB=2v8n  |  SCENE=  }}
'''WILD-TYPE STRUCTURE OF LACTOSE PERMEASE'''


==Wild-type Structure of Lactose Permease==
<StructureSection load='2v8n' size='340' side='right'caption='[[2v8n]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2v8n]] 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=2V8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V8N 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]] 3.6&#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=2v8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v8n OCA], [https://pdbe.org/2v8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v8n RCSB], [https://www.ebi.ac.uk/pdbsum/2v8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v8n 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/v8/2v8n_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=2v8n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here we describe an x-ray structure of wild-type lactose permease (LacY) from Escherichia coli determined by manipulating phospholipid content during crystallization. The structure exhibits the same global fold as the previous x-ray structures of a mutant that binds sugar but cannot catalyze translocation across the membrane. LacY is organized into two six-helix bundles with twofold pseudosymmetry separated by a large interior hydrophilic cavity open only to the cytoplasmic side and containing the side chains important for sugar and H(+) binding. To initiate transport, binding of sugar and/or an H(+) electrochemical gradient increases the probability of opening on the periplasmic side. Because the inward-facing conformation represents the lowest free-energy state, the rate-limiting step for transport may be the conformational change leading to the outward-facing conformation.


==Overview==
Structural determination of wild-type lactose permease.,Guan L, Mirza O, Verner G, Iwata S, Kaback HR Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15294-8. Epub 2007 Sep 19. PMID:17881559<ref>PMID:17881559</ref>
Here we describe an x-ray structure of wild-type lactose permease (LacY) from Escherichia coli determined by manipulating phospholipid content during crystallization. The structure exhibits the same global fold as the previous x-ray structures of a mutant that binds sugar but cannot catalyze translocation across the membrane. LacY is organized into two six-helix bundles with twofold pseudosymmetry separated by a large interior hydrophilic cavity open only to the cytoplasmic side and containing the side chains important for sugar and H(+) binding. To initiate transport, binding of sugar and/or an H(+) electrochemical gradient increases the probability of opening on the periplasmic side. Because the inward-facing conformation represents the lowest free-energy state, the rate-limiting step for transport may be the conformational change leading to the outward-facing conformation.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2V8N 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=2V8N OCA].
</div>
<div class="pdbe-citations 2v8n" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural determination of wild-type lactose permease., Guan L, Mirza O, Verner G, Iwata S, Kaback HR, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15294-8. Epub 2007 Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17881559 17881559]
*[[Lactose Permease|Lactose Permease]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Guan, L.]]
[[Category: Guan L]]
[[Category: Iwata, S.]]
[[Category: Iwata S]]
[[Category: Kaback, H R.]]
[[Category: Kaback HR]]
[[Category: Mirza, O.]]
[[Category: Mirza O]]
[[Category: Verner, G.]]
[[Category: Verner G]]
[[Category: Formylation]]
[[Category: Inner membrane]]
[[Category: Membrane]]
[[Category: Sugar transport]]
[[Category: Symport]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:22:33 2008''

Latest revision as of 15:09, 13 December 2023

Wild-type Structure of Lactose Permease

2v8n, resolution 3.60Å

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