2n6l

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'''Unreleased structure'''
 
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The entry 2n6l is ON HOLD until Paper Publication
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==Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa==
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<StructureSection load='2n6l' size='340' side='right'caption='[[2n6l]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2n6l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N6L FirstGlance]. <br>
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</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=2n6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6l OCA], [https://pdbe.org/2n6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6l RCSB], [https://www.ebi.ac.uk/pdbsum/2n6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9HWW1_PSEAE Q9HWW1_PSEAE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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OprG is an outer membrane protein of Pseudomonas aeruginosa whose function as an antibiotic-sensitive porin has been controversial and not well defined. Circumstantial evidence led to the proposal that OprG might transport hydrophobic compounds by using a lateral gate in the barrel wall thought to be lined by three conserved prolines. To test this hypothesis and to find the physiological substrates of OprG, we reconstituted the purified protein into liposomes and found it to facilitate the transport of small amino acids such as glycine, alanine, valine, and serine, which was confirmed by Pseudomonas growth assays. The structures of wild-type and a critical proline mutant were determined by nuclear magnetic resonance in dihexanoyl-phosphatidylcholine micellar solutions. Both proteins formed eight-stranded beta-barrels with flexible extracellular loops. The interfacial prolines did not form a lateral gate in these structures, but loop 3 exhibited restricted motions in the inactive P92A mutant but not in wild-type OprG.
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Authors: Kucharska, I., Seelheim, P., Edrington, T.C., Liang, B., Tamm, L.K.
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OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa.,Kucharska I, Seelheim P, Edrington T, Liang B, Tamm LK Structure. 2015 Dec 1;23(12):2234-45. doi: 10.1016/j.str.2015.10.009. Epub 2015, Nov 19. PMID:26655471<ref>PMID:26655471</ref>
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Description: Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kucharska, I]]
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<div class="pdbe-citations 2n6l" style="background-color:#fffaf0;"></div>
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[[Category: Edrington, T.C]]
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== References ==
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[[Category: Seelheim, P]]
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<references/>
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[[Category: Liang, B]]
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__TOC__
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[[Category: Tamm, L.K]]
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Edrington TC]]
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[[Category: Kucharska I]]
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[[Category: Liang B]]
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[[Category: Seelheim P]]
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[[Category: Tamm LK]]

Current revision

Solution NMR structure of Outer Membrane Protein G from Pseudomonas aeruginosa

PDB ID 2n6l

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