View source for 3wp5


==The crystal structure of mutant CDBFV E109A from Neocallimastix patriciarum==
<StructureSection load='3wp5' size='340' side='right'caption='[[3wp5]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wp5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neocallimastix_patriciarum Neocallimastix patriciarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WP5 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]] 1.32&#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=3wp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp5 OCA], [https://pdbe.org/3wp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wp5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wp5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYNC_NEOPA XYNC_NEOPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalytic domain of XynCDBFV, a glycoside hydrolase family 11 (GH11) xylanase from ruminal fungus Neocallimastix patriciarum previously engineered to exhibit higher specific activity and broader pH adaptability, holds great potential in commercial applications. Here, the crystal structures of XynCDBFV and its complex with substrate were determined to 1.27-1.43 A resolution. These structures revealed a typical GH11 beta-jelly-roll fold and detailed interaction networks between the enzyme and ligands. Notably, an extended N-terminal region (NTR) consisting of 11 amino acids was identified in the XynCDBFV structure, which is found unique among GH11 xylanases. The NTR is attached to the catalytic core by hydrogen bonds and stacking forces along with a disulfide bond between Cys-4 and Cys-172. Interestingly, the NTR deletion mutant retained 61.5% and 19.5% enzymatic activity at 55 degrees C and 75 degrees C, respectively, compared with the wild-type enzyme, whereas the C4A/C172A mutant showed 86.8% and 23.3% activity. These results suggest that NTR plays a role in XynCDBFV thermostability, and the Cys-4/Cys-172 disulfide bond is critical to the NTR-mediated interactions. Furthermore, we also demonstrated that Pichia pastoris produces XynCDBFV with higher catalytic activity at higher temperature than Escherichia coli, in which incorrect NTR folding and inefficient disulfide bond formation might have occurred. In conclusion, these structural and functional analyses of the industrially favored XynCDBFV provide a molecular basis of NTR contribution to its thermostability.

Structural analysis of a glycoside hydrolase family 11 xylanase from Neocallimastix patriciarum: insights into the molecular basis of a thermophilic enzyme.,Cheng YS, Chen CC, Huang CH, Ko TP, Luo W, Huang JW, Liu JR, Guo RT J Biol Chem. 2014 Apr 18;289(16):11020-8. doi: 10.1074/jbc.M114.550905. Epub 2014, Mar 11. PMID:24619408<ref>PMID:24619408</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wp5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neocallimastix patriciarum]]
[[Category: Chen CC]]
[[Category: Cheng YS]]
[[Category: Guo RT]]
[[Category: Huang CH]]
[[Category: Huang JW]]
[[Category: Huang TY]]
[[Category: Ko TP]]
[[Category: Liu JR]]
[[Category: Wu TH]]