5oht

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m (Protected "5oht" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5oht is ON HOLD until Paper Publication
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==GH31 glycosidase with an inhibitor bound==
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<StructureSection load='5oht' size='340' side='right' caption='[[5oht]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
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Authors: Jin, Y., Williams, S.J., Goddard-Borger, E., Davies, G.J.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5oht]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OHT FirstGlance]. <br>
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Description: GH31 glycosidase with an inhibitor bound
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9VH:[(3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)piperidin-3-yl]methanesulfonic+acid'>9VH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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[[Category: Unreleased Structures]]
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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/Sulfoquinovosidase Sulfoquinovosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.199 3.2.1.199] </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=5oht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oht OCA], [http://pdbe.org/5oht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oht RCSB], [http://www.ebi.ac.uk/pdbsum/5oht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oht ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Sulfoquinovosidase]]
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[[Category: Davies, G J]]
[[Category: Goddard-Borger, E]]
[[Category: Goddard-Borger, E]]
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[[Category: Davies, G.J]]
 
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[[Category: Williams, S.J]]
 
[[Category: Jin, Y]]
[[Category: Jin, Y]]
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[[Category: Williams, S J]]
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[[Category: Complex]]
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[[Category: General acid-base varient]]
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[[Category: Hydrolase]]
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[[Category: Sulfoglycolysis]]
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[[Category: Sulfoglycosidase]]

Revision as of 21:14, 9 August 2018

GH31 glycosidase with an inhibitor bound

5oht, resolution 1.87Å

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