View source for 4yzp


==Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4-glucanase from Bacillus licheniformis==
<StructureSection load='4yzp' size='340' side='right'caption='[[4yzp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yzp]] 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=4YZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZP 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]] 1.7&#8491;</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=4yzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzp OCA], [https://pdbe.org/4yzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yzp RCSB], [https://www.ebi.ac.uk/pdbsum/4yzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q65JI7_BACLD Q65JI7_BACLD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside 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<ref>PMID:27032335</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yzp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus licheniformis]]
[[Category: Large Structures]]
[[Category: Liberato MV]]
[[Category: Polikarpov I]]
[[Category: Popov A]]