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4xig

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Current revision (09:02, 20 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xig]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp. Sphingomonas sp.] and [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=4XIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIG FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xig]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp. Sphingomonas sp.] and [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=4XIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XIG FirstGlance]. <br>
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</td></tr><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>, <scene name='pdbligand=MAW:4-DEOXY-ALPHA-L-ERYTHRO-HEX-4-ENOPYRANURONIC+ACID'>MAW</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.402&#8491;</td></tr>
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<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>, <scene name='pdbligand=MAW:4-DEOXY-ALPHA-L-ERYTHRO-HEX-4-ENOPYRANURONIC+ACID'>MAW</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=4xig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xig OCA], [https://pdbe.org/4xig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xig RCSB], [https://www.ebi.ac.uk/pdbsum/4xig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xig ProSAT]</span></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=4xig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xig OCA], [https://pdbe.org/4xig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xig RCSB], [https://www.ebi.ac.uk/pdbsum/4xig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xig ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q9KWT8_SPHSX Q9KWT8_SPHSX]
[https://www.uniprot.org/uniprot/Q9KWT8_SPHSX Q9KWT8_SPHSX]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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 &gt;/= 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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4xig" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of bacterial alginate ABC transporter determined through humid air and glue-coating method

PDB ID 4xig

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