View source for 3sys


==Improved crystal structure of Pseudomonas aeruginosa OccK1 (OpdK)==
<StructureSection load='3sys' size='340' side='right'caption='[[3sys]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sys]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SYS FirstGlance]. <br>
</td></tr><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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=VNL:4-HYDROXY-3-METHOXYBENZOATE'>VNL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sy7|3sy7]], [[3sy9|3sy9]], [[3syb|3syb]], [[3t24|3t24]], [[3t20|3t20]], [[3szd|3szd]], [[3szv|3szv]], [[3t0s|3t0s]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">opdK, PA4898 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=3sys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sys OCA], [https://pdbe.org/3sys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sys RCSB], [https://www.ebi.ac.uk/pdbsum/3sys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sys ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Many Gram-negative bacteria, including human pathogens such as Pseudomonas aeruginosa, do not have large-channel porins. This results in an outer membrane (OM) that is highly impermeable to small polar molecules, making the bacteria intrinsically resistant towards many antibiotics. In such microorganisms, the majority of small molecules are taken up by members of the OprD outer membrane protein family. Here we show that OprD channels require a carboxyl group in the substrate for efficient transport, and based on this we have renamed the family Occ, for outer membrane carboxylate channels. We further show that Occ channels can be divided into two subfamilies, based on their very different substrate specificities. Our results rationalize how certain bacteria can efficiently take up a variety of substrates under nutrient-poor conditions without compromising membrane permeability. In addition, they explain how channel inactivation in response to antibiotics can cause resistance but does not lead to decreased fitness.

Substrate Specificity within a Family of Outer Membrane Carboxylate Channels.,Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, van den Berg B PLoS Biol. 2012 Jan;10(1):e1001242. Epub 2012 Jan 17. PMID:22272184<ref>PMID:22272184</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3sys" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Berg, B van den]]
[[Category: Eren, E]]
[[Category: Bacterial outer membrane]]
[[Category: Beta-barrel]]
[[Category: Channel]]
[[Category: Membrane protein]]