4xtc: Difference between revisions
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==Crystal structure of bacterial alginate ABC transporter in complex with alginate pentasaccharide-bound periplasmic protein== | ==Crystal structure of bacterial alginate ABC transporter in complex with alginate pentasaccharide-bound periplasmic protein== | ||
<StructureSection load='4xtc' size='340' side='right' caption='[[4xtc]], [[Resolution|resolution]] 3.60Å' scene=''> | <StructureSection load='4xtc' size='340' side='right'caption='[[4xtc]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xtc]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XTC OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4xtc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._A1 Sphingomonas sp. A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XTC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEM:BETA-D-MANNURONIC+ACID'>BEM</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]] 3.6Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEM:BETA-D-MANNURONIC+ACID'>BEM</scene></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=4xtc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xtc OCA], [https://pdbe.org/4xtc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xtc RCSB], [https://www.ebi.ac.uk/pdbsum/4xtc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xtc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9KWT8_SPHSX Q9KWT8_SPHSX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Gram-negative bacterium Sphingomonas sp. A1 incorporates alginate into cells via the cell-surface pit without prior depolymerization by extracellular enzymes. Alginate import across cytoplasmic membranes thereby depends on the ATP-binding cassette transporter AlgM1M2SS (a heterotetramer of AlgM1, AlgM2, and AlgS), which cooperates with the periplasmic solute-binding protein AlgQ1 or AlgQ2; however, several details of AlgM1M2SS-mediated alginate import are not well-understood. Herein, we analyzed ATPase and transport activities of AlgM1M2SS after reconstitution into liposomes with AlgQ2 and alginate oligosaccharide substrates having different polymerization degrees (PDs). Longer alginate oligosaccharides (PD >/= 5) stimulated the ATPase activity of AlgM1M2SS but were inert as substrates of AlgM1M2SS-mediated transport, indicating that AlgM1M2SS-mediated ATP hydrolysis can be stimulated independently of substrate transport. Using X-ray crystallography in the presence of AlgQ2 and long alginate oligosaccharides (PD 6-8) and with the humid air and glue-coating method, we determined the crystal structure of AlgM1M2SS in complex with oligosaccharide-bound AlgQ2 at 3.6 A resolution. The structure of the ATP-binding cassette transporter in complex with non-transport ligand-bound periplasmic solute-binding protein revealed that AlgM1M2SS and AlgQ2 adopt inward-facing and closed conformations, respectively. These in vitro assays and structural analyses indicated that interactions between AlgM1M2SS in the inward-facing conformation and periplasmic ligand-bound AlgQ2 in the closed conformation induce ATP hydrolysis by the ATP-binding protein AlgS. We conclude that substrate-bound AlgQ2 in the closed conformation initially interacts with AlgM1M2SS, the AlgM1M2SS-AlgQ2 complex then forms, and this formation is followed by ATP hydrolysis. | |||
A solute-binding protein in the closed conformation induces ATP hydrolysis in a bacterial ATP-binding cassette transporter involved in the import of alginate.,Kaneko A, Uenishi K, Maruyama Y, Mizuno N, Baba S, Kumasaka T, Mikami B, Murata K, Hashimoto W J Biol Chem. 2017 Sep 22;292(38):15681-15690. doi: 10.1074/jbc.M117.793992. Epub , 2017 Aug 2. PMID:28768763<ref>PMID:28768763</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xtc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baba | [[Category: Large Structures]] | ||
[[Category: Hashimoto | [[Category: Sphingomonas sp. A1]] | ||
[[Category: Kaneko | [[Category: Baba S]] | ||
[[Category: Kumasaka | [[Category: Hashimoto W]] | ||
[[Category: Maruyama | [[Category: Kaneko A]] | ||
[[Category: Mikami | [[Category: Kumasaka T]] | ||
[[Category: Mizuno | [[Category: Maruyama Y]] | ||
[[Category: Murata | [[Category: Mikami B]] | ||
[[Category: Mizuno N]] | |||
[[Category: Murata K]] | |||
