View source for 6uqj


==Crystal structure of the GH39 enzyme from Xanthomonas axonopodis pv. citri==
<StructureSection load='6uqj' size='340' side='right'caption='[[6uqj]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uqj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri_pv._citri_str._306 Xanthomonas citri pv. citri str. 306]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UQJ 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]] 1.707&#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=6uqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uqj OCA], [https://pdbe.org/6uqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uqj RCSB], [https://www.ebi.ac.uk/pdbsum/6uqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uqj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8PFC5_XANAC Q8PFC5_XANAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycoside hydrolase family 39 (GH39) is a functionally expanding family with limited understanding about the molecular basis for substrate specificity and extremophilicity. In this work, we demonstrate the key role of the positive-subsite region in modulating substrate affinity and how the lack of a C-terminal extension impacts on oligomerization and structural stability of some GH39 members. The crystallographic and SAXS structures of a new GH39 member from the phytopathogen Xanthomonas citri support the importance of an extended C-terminal to promote oligomerization as a molecular strategy to enhance thermal stability. Comparative structural analysis along with site-directed mutagenesis showed that two residues located at the positive-subsite region, Lys166 and Asp167, are critical to substrate affinity and catalytic performance, by inducing local changes in the active site for substrate binding. These findings expand the molecular understanding of the mechanisms involved in substrate recognition and structural stability of the GH39 family, which might be instrumental for biological insights, rational enzyme engineering and utilization in biorefineries.

Exploring the Molecular Basis for Substrate Affinity and Structural Stability in Bacterial GH39 beta-Xylosidases.,de Morais MAB, Polo CC, Domingues MN, Persinoti GF, Pirolla RAS, de Souza FHM, Correa JBL, Dos Santos CR, Murakami MT Front Bioeng Biotechnol. 2020 May 15;8:419. doi: 10.3389/fbioe.2020.00419., eCollection 2020. PMID:32500063<ref>PMID:32500063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6uqj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Xylosidase 3D structures|Xylosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthomonas citri pv. citri str. 306]]
[[Category: Morais MAB]]
[[Category: Murakami MT]]
[[Category: Polo CC]]
[[Category: Santos CR]]