2cfq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2cfq.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2cfq", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2cfq|  PDB=2cfq  |  SCENE=  }}
'''SUGAR FREE LACTOSE PERMEASE AT NEUTRAL PH'''


==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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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>
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.


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


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/16525509 16525509]
*[[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: Lactose permease]]
[[Category: Lactose/h+ symport]]
[[Category: Sugar transport]]
[[Category: Transmembrane]]
[[Category: Transport mechanism]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:01:57 2008''
Retrieved from "https://proteopedia.org/2cfq"