5aee

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==A bacterial protein structure in glycoside hydrolase family 31==
==A bacterial protein structure in glycoside hydrolase family 31==
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<StructureSection load='5aee' size='340' side='right' caption='[[5aee]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='5aee' size='340' side='right'caption='[[5aee]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5aee]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AEE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5aee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AEE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NSQ:4-NITROPHENYL-ALPHA-D-SULFOQUINOVOSIDE'>NSQ</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]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aed|5aed]], [[5aeg|5aeg]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NSQ:4-NITROPHENYL-ALPHA-D-SULFOQUINOVOSIDE'>NSQ</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5aee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aee OCA], [https://pdbe.org/5aee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aee RCSB], [https://www.ebi.ac.uk/pdbsum/5aee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aee ProSAT]</span></td></tr>
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<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=5aee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aee OCA], [http://pdbe.org/5aee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aee RCSB], [http://www.ebi.ac.uk/pdbsum/5aee PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/YIHQ_ECOLI YIHQ_ECOLI]] Exhibits hydrolysis activity against alpha-glucosyl fluoride, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed.<ref>PMID:15294295</ref>
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[https://www.uniprot.org/uniprot/SQASE_ECOLI SQASE_ECOLI] Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup found in ubiquitous plant sulfolipids. Is also able to hydrolyze simple sulfoquinovosides such as 1-sulfoquinovosylglycerol (SQGro). Is a retaining glycoside hydrolase, since it forms the alpha anomer of SQ (PubMed:26878550). Also exhibits some alpha-glucosidase activity against alpha-glucosyl fluoride in vitro, although natural substrates, such as alpha-glucobioses are scarcely hydrolyzed (PubMed:15294295).<ref>PMID:15294295</ref> <ref>PMID:26878550</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5aee" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5aee" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
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*[[Art:Molecular Sculpture|Art:Molecular Sculpture]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alpha-glucosidase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Davies, G J]]
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[[Category: Large Structures]]
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[[Category: Goddard-Borger, E D]]
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[[Category: Davies GJ]]
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[[Category: Jin, Y]]
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[[Category: Goddard-Borger ED]]
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[[Category: Speciale, G]]
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[[Category: Jin Y]]
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[[Category: Williams, S J]]
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[[Category: Speciale G]]
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[[Category: Alpha-sulfoquinovosidase]]
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[[Category: Williams SJ]]
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[[Category: Gh31]]
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[[Category: Hydrolase]]
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Current revision

A bacterial protein structure in glycoside hydrolase family 31

PDB ID 5aee

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