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== | ==Structure of endo-beta-N-acetylglucosaminidase A== | ||
[[3fhq]] is a 4 chain structure with sequence from [ | <StructureSection load='3fhq' size='340' side='right'caption='[[3fhq]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fhq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Glutamicibacter_protophormiae Glutamicibacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHQ 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]] 2.452Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NGT:3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL'>NGT</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=3fhq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhq OCA], [https://pdbe.org/3fhq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhq RCSB], [https://www.ebi.ac.uk/pdbsum/3fhq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9ZB22_9MICC Q9ZB22_9MICC] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/3fhq_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fhq ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis of glycopeptides. We have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A) in 3 forms, one in native form, one in complex with Man(3)GlcNAc-thiazoline and another in complex with GlcNAc-Asn. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. The conserved essential catalytic residues - E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as "gate-keepers". Interestingly, Y299F mutation resulted in a 3 fold increase in the transglycosylation activity. The structure provides insights into the catalytic mechanism of GH85 family of glycoside hydrolases at molecular level and could assist rational engineering of ENGases. | |||
Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.,Yin J, Li L, Shaw N, Li Y, Song JK, Zhang W, Xia C, Zhang R, Joachimiak A, Zhang HC, Wang LX, Liu ZJ, Wang P PLoS ONE. 2009;4(3):e4658. Epub 2009 Mar 2. PMID:19252736<ref>PMID:19252736</ref> | |||
<ref | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
[[Category: Jie | <div class="pdbe-citations 3fhq" style="background-color:#fffaf0;"></div> | ||
[[Category: Joachimiak | == References == | ||
[[Category: Li | <references/> | ||
[[Category: Li | __TOC__ | ||
[[Category: Liu | </StructureSection> | ||
[[Category: Shaw | [[Category: Glutamicibacter protophormiae]] | ||
[[Category: Song | [[Category: Large Structures]] | ||
[[Category: Wang | [[Category: Jie Y]] | ||
[[Category: Wang | [[Category: Joachimiak A]] | ||
[[Category: Xia | [[Category: Li L]] | ||
[[Category: Zhang | [[Category: Li Y]] | ||
[[Category: Zhang | [[Category: Liu Z-J]] | ||
[[Category: Zhang | [[Category: Shaw N]] | ||
[[Category: Song J]] | |||
[[Category: Wang L-X]] | |||
[[Category: Wang P]] | |||
[[Category: Xia C]] | |||
[[Category: Zhang H-C]] | |||
[[Category: Zhang R]] | |||
[[Category: Zhang W]] | |||
Latest revision as of 18:29, 1 November 2023
Structure of endo-beta-N-acetylglucosaminidase AStructure of endo-beta-N-acetylglucosaminidase A
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEndo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis of glycopeptides. We have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A) in 3 forms, one in native form, one in complex with Man(3)GlcNAc-thiazoline and another in complex with GlcNAc-Asn. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. The conserved essential catalytic residues - E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as "gate-keepers". Interestingly, Y299F mutation resulted in a 3 fold increase in the transglycosylation activity. The structure provides insights into the catalytic mechanism of GH85 family of glycoside hydrolases at molecular level and could assist rational engineering of ENGases. Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A.,Yin J, Li L, Shaw N, Li Y, Song JK, Zhang W, Xia C, Zhang R, Joachimiak A, Zhang HC, Wang LX, Liu ZJ, Wang P PLoS ONE. 2009;4(3):e4658. Epub 2009 Mar 2. PMID:19252736[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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