View source for 9gci


==The crystal structure of beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus determined at 1.47 A resolution==
<StructureSection load='9gci' size='340' side='right'caption='[[9gci]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldicellulosiruptor_saccharolyticus_DSM_8903 Caldicellulosiruptor saccharolyticus DSM 8903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GCI 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]] 1.47&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=9gci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gci OCA], [https://pdbe.org/9gci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gci RCSB], [https://www.ebi.ac.uk/pdbsum/9gci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gci ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4XIG7_CALS8 A4XIG7_CALS8] 
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== Publication Abstract from PubMed ==
beta-Glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus (Bgl1) has been denoted as having an attractive catalytic profile for various industrial applications. Bgl1 catalyses the final step of in the decomposition of cellulose, an unbranched glucose polymer that has attracted the attention of researchers in recent years as it is the most abundant renewable source of reduced carbon in the biosphere. With the aim of enhancing the thermostability of Bgl1 for a broad spectrum of biotechnological processes, it has been subjected to structural studies. Crystal structures of Bgl1 and its complex with glucose were determined at 1.47 and 1.95 A resolution, respectively. Bgl1 is a member of glycosyl hydrolase family 1 (GH1 superfamily, EC 3.2.1.21) and the results showed that the 3D structure of Bgl1 follows the overall architecture of the GH1 family, with a classical (beta/alpha)(8) TIM-barrel fold. Comparisons of Bgl1 with sequence or structural homologues of beta-glucosidase reveal quite similar structures but also unique structural features in Bgl1 with plausible functional roles.

Structural studies of beta-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus.,Sotiropoulou AI, Hatzinikolaou DG, Chrysina ED Acta Crystallogr D Struct Biol. 2024 Oct 1;80(Pt 10):733-743. doi: , 10.1107/S2059798324009252. Epub 2024 Oct 1. PMID:39361356<ref>PMID:39361356</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9gci" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Caldicellulosiruptor saccharolyticus DSM 8903]]
[[Category: Large Structures]]
[[Category: Chrysina ED]]
[[Category: Sotiropoulou AI]]