1fx8

<StructureSection load='1fx8' size='340' side='right' caption='[[1fx8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fx8]] is a 1 chain structure with 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=1FX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FX8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fx8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fx8 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/GLPF_ECOLI GLPF_ECOLI]] Transporter of glycerol across the cytoplasmic membrane, with limited permeability to water and small uncharged compounds such as polyols.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/1fx8_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Membrane channel proteins of the aquaporin family are highly selective for permeation of specific small molecules, with absolute exclusion of ions and charged solutes and without dissipation of the electrochemical potential across the cell membrane. We report the crystal structure of the Escherichia coli glycerol facilitator (GlpF) with its primary permeant substrate glycerol at 2.2 angstrom resolution. Glycerol molecules line up in an amphipathic channel in single file. In the narrow selectivity filter of the channel the glycerol alkyl backbone is wedged against a hydrophobic corner, and successive hydroxyl groups form hydrogen bonds with a pair of acceptor, and donor atoms. Two conserved aspartic acid-proline-alanine motifs form a key interface between two gene-duplicated segments that each encode three-and-one-half membrane-spanning helices around the channel. This structure elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.

Structure of a glycerol-conducting channel and the basis for its selectivity.,Fu D, Libson A, Miercke LJ, Weitzman C, Nollert P, Krucinski J, Stroud RM Science. 2000 Oct 20;290(5491):481-6. PMID:11039922<ref>PMID:11039922</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Aquaporin|Aquaporin]]

*[[Ion channels|Ion channels]]

[[Category: Fu, D]]

[[Category: Libson, A]]

[[Category: Miercke, L J.W]]

[[Category: Nollert, P]]

[[Category: Stroud, R M]]

[[Category: Weitzman, C]]

[[Category: Glycerol-conducting membrane channel protein]]

[[Category: Membrane protein]]