8qqh
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of beta-galactosidase from Desulfurococcus amyloliticus== | |
| + | <StructureSection load='8qqh' size='340' side='right'caption='[[8qqh]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8qqh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfurococcus_amylolyticus Desulfurococcus amylolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QQH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=8qqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qqh OCA], [https://pdbe.org/8qqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qqh RCSB], [https://www.ebi.ac.uk/pdbsum/8qqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qqh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B8D3P7_DESA1 B8D3P7_DESA1] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The most extensively studied beta-d-galactosidases (EC3.2.1.23) belonging to four glycoside hydrolase (GH) families 1, 2, 35, and 42 are widely distributed among Bacteria, Archaea and Eukaryotes. Here, we report a novel GH35 family beta-galactosidase from the hyperthermophilic Thermoprotei archaeon Desulfurococcus amylolyticus (DabetaGal). Unlike fungal monomeric six-domain beta-galactosidases, the DabetaGal enzyme is a dimer; it has an extra jelly roll domain D7 and three composite domains (D4, D5, and D6) that are formed by the distantly located polypeptide chain regions. The enzyme possesses a high specificity for beta-d-galactopyranosides, and its distinguishing feature is the ability to cleave pNP-beta-d-fucopyranoside. DabetaGal efficiently catalyzes the hydrolysis of lactose at high temperatures, remains stable and active at 65 degrees capital ES, Cyrillic, and retains activity at 95 degrees capital ES, Cyrillic with a half-life time value equal to 73 min. These properties make archaeal DabetaGal a more attractive candidate for biotechnology than the widely used fungal beta-galactosidases. | ||
| - | + | The archaeal highly thermostable GH35 family beta-galactosidase DabetaGal has a unique seven domain protein fold.,Kil Y, Pichkur EB, Sergeev VR, Zabrodskaya Y, Myasnikov A, Konevega AL, Shtam T, Samygina VR, Rychkov GN FEBS J. 2024 Jun 2. doi: 10.1111/febs.17166. PMID:38825733<ref>PMID:38825733</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8qqh" style="background-color:#fffaf0;"></div> |
| - | [[Category: Kil | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Samygina | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Desulfurococcus amylolyticus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kil Y]] | ||
| + | [[Category: Rychkov GN]] | ||
| + | [[Category: Samygina VR]] | ||
| + | [[Category: Sergeev RS]] | ||
Current revision
Structure of beta-galactosidase from Desulfurococcus amyloliticus
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