4yzt: Difference between revisions

Line 9:

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzt OCA], [http://pdbe.org/4yzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yzt RCSB], [http://www.ebi.ac.uk/pdbsum/4yzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzt ProSAT]</span></td></tr>

</table>

== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 9: / Line 9: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzt OCA], [http://pdbe.org/4yzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yzt RCSB], [http://www.ebi.ac.uk/pdbsum/4yzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzt ProSAT]</span></td></tr>
 </table>
+<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 4yzt" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>