6jqf: Difference between revisions
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==Crystallization analysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila== | |||
<StructureSection load='6jqf' size='340' side='right'caption='[[6jqf]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jqf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JQF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jqf OCA], [http://pdbe.org/6jqf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jqf RCSB], [http://www.ebi.ac.uk/pdbsum/6jqf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jqf ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this paper, we characterized Am2136 as a beta-N-acetylhexosaminidase from Akkermansia muciniphila to perform the biochemical characteristics and the crystal structure of selenomethionine-labeled Am2136 with GlcNAc complex. Crystallographic evidence suggests that an oxazolinium ion was formed intermediately by the 2-acetamido group during the substrate-assisted catalytic procedure. Structural and kinetic analysis of native Am2136 and D412A, E413A mutants were investigated and the results revealed substantial difference. The Kcat/Km value of D412A was decreased 4297-fold compared to native Am2136 revealed that mutation of Asp-412 results in preventing the 2-acetamido substituent from providing anchimeric assistance and thus reducing the catalytic efficiency. Moreover, Am2136 has a wide dependence on pH and temperature, while sensitive to divalent metal ions such as Ca(2+) and Mn(2+). These biochemical and crystallographic results provide evidences that Asp-412 residue assists to orient the 2-acetamido group for catalysis. Based on crystallographic evidence and sequence alignment with other GH family 20 enzymes, Asp-412 residue is possibly fundamental for Am2136 during substrate-assisted catalysis. | |||
Biochemical characteristics and crystallographic evidence for substrate-assisted catalysis of a beta-N-acetylhexosaminidase in Akkermansia muciniphila.,Chen X, Li M, Wang Y, Tang R, Zhang M Biochem Biophys Res Commun. 2019 Sep 10;517(1):29-35. doi:, 10.1016/j.bbrc.2019.06.150. Epub 2019 Jul 23. PMID:31345574<ref>PMID:31345574</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6jqf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chen, X]] | |||
[[Category: Zhang, M]] | [[Category: Zhang, M]] | ||
[[Category: | [[Category: Akkermansia muciniphila]] | ||
[[Category: Catalytic mechanism]] | |||
[[Category: Crystallographic evidence]] | |||
[[Category: Hydrolase]] | |||
[[Category: Keywords:beta-n-acetylhexosaminida]] | |||
Revision as of 15:04, 11 December 2019
Crystallization analysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila
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