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| ==Improved crystal structure of Pseudomonas aeruginosa OprD== | | ==Improved crystal structure of Pseudomonas aeruginosa OprD== |
| <StructureSection load='3sy7' size='340' side='right' caption='[[3sy7]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='3sy7' size='340' side='right'caption='[[3sy7]], [[Resolution|resolution]] 2.15Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3sy7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SY7 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3sy7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SY7 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sy9|3sy9]], [[3syb|3syb]], [[3sys|3sys]], [[3szd|3szd]], [[3szv|3szv]], [[3t0s|3t0s]], [[3t20|3t20]], [[2odj|2odj]], [[3t24|3t24]]</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></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oprD, PA0958 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</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=3sy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sy7 OCA], [https://pdbe.org/3sy7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sy7 RCSB], [https://www.ebi.ac.uk/pdbsum/3sy7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sy7 ProSAT]</span></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=3sy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sy7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sy7 RCSB], [http://www.ebi.ac.uk/pdbsum/3sy7 PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/PORD_PSEAE PORD_PSEAE] Porin with a specificity for basic amino acids. Also possesses serine protease activity.<ref>PMID:2118530</ref> <ref>PMID:8843159</ref> |
| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div> | |
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| ==See Also== | | ==See Also== |
| *[[Porin|Porin]] | | *[[Porin 3D structures|Porin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Pseudomonas aeruginosa]] | | [[Category: Pseudomonas aeruginosa]] |
| [[Category: Berg, B van den]]
| | [[Category: Eren E]] |
| [[Category: Eren, E]] | | [[Category: Van den Berg B]] |
| [[Category: Beta-barrel]] | |
| [[Category: Channel]]
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| [[Category: Membrane protein]]
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| [[Category: Outer membrane]]
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