3pgr

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m (Protected "3pgr" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 3pgr is ON HOLD until Paper Publication
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==Asp348Arg mutant of EcFadL==
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<StructureSection load='3pgr' size='340' side='right'caption='[[3pgr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3pgr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGR 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]] 2.6&#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=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</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=3pgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgr OCA], [https://pdbe.org/3pgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pgr RCSB], [https://www.ebi.ac.uk/pdbsum/3pgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FADL_ECOLI FADL_ECOLI] Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ligand-gated channels, in which a substrate transport pathway is formed as a result of the binding of a small-molecule chemical messenger, constitute a diverse class of membrane proteins with important functions in prokaryotic and eukaryotic organisms. Despite their widespread nature, no ligand-gated channels have yet been found within the outer membrane (OM) of Gram-negative bacteria. Here we show, using in vivo transport assays, intrinsic tryptophan fluorescence and X-ray crystallography, that high-affinity (submicromolar) substrate binding to the OM long-chain fatty acid transporter FadL from Escherichia coli causes conformational changes in the N terminus that open up a channel for substrate diffusion. The OM long-chain fatty acid transporter FadL from E. coli is a unique paradigm for OM diffusion-driven transport, in which ligand gating within a beta-barrel membrane protein is a prerequisite for channel formation.
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Authors: Lepore, B.W., van den Berg, B., Indic, M., Hearn, E., Patel, D., Pham, H.
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Ligand-gated diffusion across the bacterial outer membrane.,Lepore BW, Indic M, Pham H, Hearn EM, Patel DR, van den Berg B Proc Natl Acad Sci U S A. 2011 May 18. PMID:21593406<ref>PMID:21593406</ref>
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Description: Asp348Arg mutant of EcFadL
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3pgr" style="background-color:#fffaf0;"></div>
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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 K-12]]
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[[Category: Large Structures]]
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[[Category: Hearn E]]
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[[Category: Indic M]]
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[[Category: Lepore BW]]
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[[Category: Patel D]]
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[[Category: Pham H]]
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[[Category: Van den Berg B]]

Current revision

Asp348Arg mutant of EcFadL

PDB ID 3pgr

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