View source for 3x2h


==X-ray structure of PcCel45A N92D with cellopentaose at 95K.==
<StructureSection load='3x2h' size='340' side='right'caption='[[3x2h]], [[Resolution|resolution]] 0.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3x2h]] 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=3X2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2H 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]] 0.99&#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>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900016:beta-cellopentaose'>PRD_900016</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=3x2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2h OCA], [https://pdbe.org/3x2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2h RCSB], [https://www.ebi.ac.uk/pdbsum/3x2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2h 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 3x2h" 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]]