8gf3
From Proteopedia
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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=8gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gf3 OCA], [https://pdbe.org/8gf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gf3 RCSB], [https://www.ebi.ac.uk/pdbsum/8gf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gf3 ProSAT]</span></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=8gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gf3 OCA], [https://pdbe.org/8gf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gf3 RCSB], [https://www.ebi.ac.uk/pdbsum/8gf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gf3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q65JI6_BACLD Q65JI6_BACLD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glycoside hydrolase family 5 (GH5) encompasses enzymes with several different activities, including endo-1,4-beta-mannosidases. These enzymes are involved in mannan degradation, and have a number of biotechnological applications, such as mannooligosaccharide prebiotics production, stain removal and dyes decolorization, to name a few. Despite the importance of GH5 enzymes, only a few members of subfamily 7 were structurally characterized. In the present work, biochemical and structural characterization of Bacillus licheniformis GH5 mannanase, BlMan5_7 were performed and the enzyme cleavage pattern was analyzed, showing that BlMan5_7 requires at least 5 occupied subsites to perform efficient hydrolysis. Additionally, crystallographic structure at 1.3 A resolution was determined and mannoheptaose (M7) was docked into the active site to investigate the interactions between substrate and enzyme through molecular dynamic (MD) simulations, revealing the existence of a - 4 subsite, which might explain the generation of mannotetraose (M4) as an enzyme product. Biotechnological application of the enzyme in stain removal was investigated, demonstrating that BlMan5_7 addition to washing solution greatly improves mannan-based stain elimination. | ||
| + | |||
| + | Unravelling biochemical and structural features of Bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies.,Briganti L, Manzine LR, de Mello Capetti CC, de Araujo EA, de Oliveira Arnoldi Pellegrini V, Guimaraes FEG, de Oliveira Neto M, Polikarpov I Int J Biol Macromol. 2024 Aug;274(Pt 2):133182. doi: , 10.1016/j.ijbiomac.2024.133182. Epub 2024 Jun 15. PMID:38885857<ref>PMID:38885857</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8gf3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystallographic structure from BlMan5_7
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