5aed

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==A bacterial protein structure in glycoside hydrolase family 31.==
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<StructureSection load='5aed' size='340' side='right' caption='[[5aed]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
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==A bacterial protein structure in glycoside hydrolase family 31==
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<StructureSection load='5aed' size='340' side='right'caption='[[5aed]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5aed]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AED FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5aed]] 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=5AED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AED 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 1.91&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aee|5aee]], [[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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=5aed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aed OCA], [http://pdbe.org/5aed PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aed RCSB], [http://www.ebi.ac.uk/pdbsum/5aed PDBsum]</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=5aed FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aed OCA], [https://pdbe.org/5aed PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aed RCSB], [https://www.ebi.ac.uk/pdbsum/5aed PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aed ProSAT]</span></td></tr>
</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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life.
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YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids.,Speciale G, Jin Y, Davies GJ, Williams SJ, Goddard-Borger ED Nat Chem Biol. 2016 Feb 15. doi: 10.1038/nchembio.2023. PMID:26878550<ref>PMID:26878550</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 5aed" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Davies, G J]]
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[[Category: Escherichia coli K-12]]
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[[Category: Goddard-Borger, E D]]
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[[Category: Large Structures]]
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[[Category: Jin, Y]]
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[[Category: Davies GJ]]
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[[Category: Speciale, G]]
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[[Category: Goddard-Borger ED]]
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[[Category: Williams, S J]]
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[[Category: Jin Y]]
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[[Category: Alpha-sulfoquinovosidase]]
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[[Category: Speciale G]]
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[[Category: Gh31]]
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[[Category: Williams SJ]]
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[[Category: Hydrolase]]
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Current revision

A bacterial protein structure in glycoside hydrolase family 31

PDB ID 5aed

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