4yzt: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yzt]] 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=4YZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4yzt]] 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=4YZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.665Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</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=4yzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzt OCA], [https://pdbe.org/4yzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yzt RCSB], [https://www.ebi.ac.uk/pdbsum/4yzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzt 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=4yzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzt OCA], [https://pdbe.org/4yzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yzt RCSB], [https://www.ebi.ac.uk/pdbsum/4yzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:10, 27 September 2023
Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4-glucanase from Bacillus licheniformis complexed with cellotetraoseCrystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4-glucanase from Bacillus licheniformis complexed with cellotetraose
Structural highlights
FunctionPublication Abstract from PubMedGlycoside hydrolases (GHs) play fundamental roles in the decomposition of lignocellulosic biomaterials. Here, we report the full-length structure of a cellulase from Bacillus licheniformis (BlCel5B), a member of the GH5 subfamily 4 that is entirely dependent on its two ancillary modules (Ig-like module and CBM46) for catalytic activity. Using X-ray crystallography, small-angle X-ray scattering and molecular dynamics simulations, we propose that the C-terminal CBM46 caps the distal N-terminal catalytic domain (CD) to establish a fully functional active site via a combination of large-scale multidomain conformational selection and induced-fit mechanisms. The Ig-like module is pivoting the packing and unpacking motions of CBM46 relative to CD in the assembly of the binding subsite. This is the first example of a multidomain GH relying on large amplitude motions of the CBM46 for assembly of the catalytically competent form of the enzyme. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism.,Liberato MV, Silveira RL, Prates ET, de Araujo EA, Pellegrini VO, Camilo CM, Kadowaki MA, Neto Mde O, Popov A, Skaf MS, Polikarpov I Sci Rep. 2016 Apr 1;6:23473. doi: 10.1038/srep23473. PMID:27032335[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||