8gf3: Difference between revisions
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==Crystallographic structure from BlMan5_7== | |||
<StructureSection load='8gf3' size='340' side='right'caption='[[8gf3]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8gf3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GF3 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]] 1.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=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> | |||
== 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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Briganti | <div class="pdbe-citations 8gf3" style="background-color:#fffaf0;"></div> | ||
[[Category: Polikarpov | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus licheniformis]] | |||
[[Category: Large Structures]] | |||
[[Category: Araujo EA]] | |||
[[Category: Briganti L]] | |||
[[Category: Polikarpov I]] | |||
Latest revision as of 06:11, 31 July 2024
Crystallographic structure from BlMan5_7
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