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3wsc

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Current revision (08:47, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3wsc' size='340' side='right'caption='[[3wsc]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='3wsc' size='340' side='right'caption='[[3wsc]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wsc]] is a 2 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=3WSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wsc]] is a 2 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=3WSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSC FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90322 Sphingomonas sp. A1])</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]] 1.992&#8491;</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=3wsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsc OCA], [https://pdbe.org/3wsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsc RCSB], [https://www.ebi.ac.uk/pdbsum/3wsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsc 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=3wsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsc OCA], [https://pdbe.org/3wsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsc RCSB], [https://www.ebi.ac.uk/pdbsum/3wsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q25C86_9SPHN Q25C86_9SPHN]
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A gram-negative Sphingomonas sp. strain A1 inducibly forms a mouth-like pit on the cell surface in the presence of alginate and directly incorporates polymers into the cytoplasm via the pit and ABC transporter. Among the bacterial proteins involved in import of alginate, a cell-surface EfeO-like Algp7 shows an ability to bind alginate, suggesting its contribution to accumulate alginate in the pit. Here, we show identification of its positively charged cluster involved in alginate binding using X-ray crystallography, docking simulation, and site-directed mutagenesis. The tertiary structure of Algp7 was determined at a high resolution (1.99A) by molecular replacement, although no alginates were included in the structure. Thus, an in silico model of Algp7/oligoalginate was constructed by docking simulation using atomic coordinates of Algp7 and alginate oligosaccharides, where some charged residues were found to be potential candidates for alginate binding. Site-directed mutagenesis was conducted and five purified mutants K68A, K69A, E194A, N221A, and K68A/K69A were subjected to a binding assay. UV absorption difference spectroscopy along with differential scanning fluorimetry analysis indicated that K68A/K69A exhibited a significant reduction in binding affinity with alginate than wild-type Algp7. Based on these data, Lys68/Lys69 residues of Algp7 probably play an important role in binding alginate.
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Structural insights into alginate binding by bacterial cell-surface protein.,Temtrirath K, Murata K, Hashimoto W Carbohydr Res. 2014 Nov 29;404C:39-45. doi: 10.1016/j.carres.2014.11.008. PMID:25665777<ref>PMID:25665777</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 3wsc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sphingomonas sp. a1]]
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[[Category: Sphingomonas sp. A1]]
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[[Category: Hashimoto, W]]
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[[Category: Hashimoto W]]
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[[Category: Murata, K]]
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[[Category: Murata K]]
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[[Category: Temtrirath, K]]
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[[Category: Temtrirath K]]
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[[Category: Alginate binding]]
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[[Category: Alginate-binding protein]]
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[[Category: Sphingomona]]
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[[Category: Two up-and-down four-helical bundle]]
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Current revision

Crystal structure of alginate-binding protein Algp7

PDB ID 3wsc

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