View source for 4lx4


==Crystal Structure Determination of Pseudomonas stutzeri endoglucanase Cel5A using a Twinned Data Set==
<StructureSection load='4lx4' size='340' side='right'caption='[[4lx4]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lx4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri_A1501 Pseudomonas stutzeri A1501]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LX4 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]] 1.556&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4lx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lx4 OCA], [https://pdbe.org/4lx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lx4 RCSB], [https://www.ebi.ac.uk/pdbsum/4lx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lx4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4VME5_STUS1 A4VME5_STUS1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The discovery of new glycoside hydrolases that can be utilized in the chemoenzymatic synthesis of carbohydrates has emerged as a promising approach for various biotechnological processes. In this study, recombinant Ps_Cel5A from Pseudomonas stutzeri A1501, a novel member of the GH5_5 subfamily, was expressed, purified and crystallized. Preliminary experiments confirmed the ability of Ps_Cel5A to catalyze transglycosylation with cellotriose as a substrate. The crystal structure revealed several structural determinants in and around the positive subsites, providing a molecular basis for a better understanding of the mechanisms that promote and favour synthesis rather than hydrolysis. In the positive subsites, two nonconserved positively charged residues (Arg178 and Lys216) were found to interact with cellobiose. This adaptation has also been reported for transglycosylating beta-mannanases of the GH5_7 subfamily.

Crystal structure determination of Pseudomonas stutzeri A1501 endoglucanase Cel5A: the search for a molecular basis for glycosynthesis in GH5_5 enzymes.,Dutoit R, Delsaute M, Collet L, Vander Wauven C, Van Elder D, Berlemont R, Richel A, Galleni M, Bauvois C Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):605-615. doi:, 10.1107/S2059798319007113. Epub 2019 Jun 6. PMID:31205022<ref>PMID:31205022</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lx4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri A1501]]
[[Category: Bauvois C]]
[[Category: Berlemont R]]
[[Category: Delsaute M]]
[[Category: Dutoit R]]
[[Category: Galleni M]]
[[Category: Van Elder D]]