6stl: Difference between revisions
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==Taurine ABC transporter substrate binding protein TauA from E. coli in complex with taurine== | |||
<StructureSection load='6stl' size='340' side='right'caption='[[6stl]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6stl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6STL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6STL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=TAU:2-AMINOETHANESULFONIC+ACID'>TAU</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=6stl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6stl OCA], [http://pdbe.org/6stl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6stl RCSB], [http://www.ebi.ac.uk/pdbsum/6stl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6stl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/TAUA_ECOLI TAUA_ECOLI]] Part of a binding-protein-dependent transport system for taurine. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Under limiting sulfur availability, bacteria can assimilate sulfur from alkanesulfonates. Bacteria utilize ATP-binding cassette (ABC) transporters to internalise them for further processing to release sulfur. In gram-negative bacteria the TauABC and SsuABC ensure internalization, although, these two systems have common substrates, the former has been characterized as a taurine specific system. TauA and SsuA are substrate-binding proteins (SBPs) that bind and bring the alkanesulfonates to the ABC importer for transport. Here, we have determined the crystal structure of TauA and have characterized its thermodynamic binding parameters by isothermal titration calorimetry in complex with taurine and different alkanesulfonates. Our structures revealed that the coordination of the alkanesulfonates is conserved, with the exception of Asp205 that is absent from SsuA, but the thermodynamic parameters revealed a very high enthalpic penalty cost for binding of the other alkanesulfonates relative to taurine. Our molecular dynamic simulations indicated that the different levels of hydration of the binding site contributed to the selectivity for taurine over the other alkanesulfonates. Such selectivity mechanism is very likely to be employed by other SBPs of ABC transporters. | |||
Desolvation of the substrate-binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC.,Qu F, ElOmari K, Wagner A, De Simone A, Beis K Biochem J. 2019 Dec 12;476(23):3649-3660. doi: 10.1042/BCJ20190779. PMID:31802112<ref>PMID:31802112</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6stl" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Beis, K]] | |||
[[Category: ElOmari, K]] | |||
[[Category: Qu, F]] | |||
[[Category: Wagner, A]] | [[Category: Wagner, A]] | ||
[[Category: | [[Category: Abc transporter]] | ||
[[Category: | [[Category: Taurine substrate binding protein]] | ||
[[Category: Transport protein]] | |||
Latest revision as of 10:56, 18 December 2019
Taurine ABC transporter substrate binding protein TauA from E. coli in complex with taurineTaurine ABC transporter substrate binding protein TauA from E. coli in complex with taurine
Structural highlights
Function[TAUA_ECOLI] Part of a binding-protein-dependent transport system for taurine. Publication Abstract from PubMedUnder limiting sulfur availability, bacteria can assimilate sulfur from alkanesulfonates. Bacteria utilize ATP-binding cassette (ABC) transporters to internalise them for further processing to release sulfur. In gram-negative bacteria the TauABC and SsuABC ensure internalization, although, these two systems have common substrates, the former has been characterized as a taurine specific system. TauA and SsuA are substrate-binding proteins (SBPs) that bind and bring the alkanesulfonates to the ABC importer for transport. Here, we have determined the crystal structure of TauA and have characterized its thermodynamic binding parameters by isothermal titration calorimetry in complex with taurine and different alkanesulfonates. Our structures revealed that the coordination of the alkanesulfonates is conserved, with the exception of Asp205 that is absent from SsuA, but the thermodynamic parameters revealed a very high enthalpic penalty cost for binding of the other alkanesulfonates relative to taurine. Our molecular dynamic simulations indicated that the different levels of hydration of the binding site contributed to the selectivity for taurine over the other alkanesulfonates. Such selectivity mechanism is very likely to be employed by other SBPs of ABC transporters. Desolvation of the substrate-binding protein TauA dictates ligand specificity for the alkanesulfonate ABC importer TauABC.,Qu F, ElOmari K, Wagner A, De Simone A, Beis K Biochem J. 2019 Dec 12;476(23):3649-3660. doi: 10.1042/BCJ20190779. PMID:31802112[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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