View source for 3x2j


==X-ray structure of PcCel45A D114N apo form at 95K.==
<StructureSection load='3x2j' size='340' side='right'caption='[[3x2j]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3x2j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X2J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2J 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]] 1.301&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=40S:3-METHYLPENTANE-1,5-DIOL'>40S</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=3x2j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2j OCA], [https://pdbe.org/3x2j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2j RCSB], [https://www.ebi.ac.uk/pdbsum/3x2j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B3Y002_PHACH B3Y002_PHACH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the "Newton's cradle"-like proton relay pathway of the catalytic cycle. Amide-imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions.

"Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography.,Nakamura A, Ishida T, Kusaka K, Yamada T, Fushinobu S, Tanaka I, Kaneko S, Ohta K, Tanaka H, Inaka K, Higuchi Y, Niimura N, Samejima M, Igarashi K Sci Adv. 2015 Aug 21;1(7):e1500263. doi: 10.1126/sciadv.1500263. eCollection 2015, Aug. PMID:26601228<ref>PMID:26601228</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3x2j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phanerodontia chrysosporium]]
[[Category: Igarashi K]]
[[Category: Ishida T]]
[[Category: Nakamura A]]
[[Category: Samejima M]]