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2vtf

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Current revision (10:04, 9 May 2024) (edit) (undo)
 
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==X-RAY CRYSTAL STRUCTURE OF THE ENDO-BETA-N-ACETYLGLUCOSAMINIDASE FROM ARTHROBACTER PROTOPHORMIAE E173Q MUTANT REVEALS A TIM BARREL CATALYTIC DOMAIN AND TWO ANCILLARY DOMAINS==
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<StructureSection load='2vtf' size='340' side='right' caption='[[2vtf]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
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==X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains==
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<StructureSection load='2vtf' size='340' side='right'caption='[[2vtf]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vtf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTF OCA]. <br>
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<table><tr><td colspan='2'>[[2vtf]] is a 2 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=2VTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTF FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B3P:2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>B3P</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vtf RCSB], [http://www.ebi.ac.uk/pdbsum/2vtf PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtf OCA], [https://pdbe.org/2vtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vtf RCSB], [https://www.ebi.ac.uk/pdbsum/2vtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vtf ProSAT]</span></td></tr>
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<table>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9ZB22_9MICC Q9ZB22_9MICC]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vtf_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vtf_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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</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=2vtf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity.,Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, Taylor EJ J Mol Biol. 2009 May 29;389(1):1-9. Epub 2009 Mar 24. PMID:19327363<ref>PMID:19327363</ref>
The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity.,Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, Taylor EJ J Mol Biol. 2009 May 29;389(1):1-9. Epub 2009 Mar 24. PMID:19327363<ref>PMID:19327363</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2vtf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arthrobacter protophormiae]]
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[[Category: Glutamicibacter protophormiae]]
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[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[[Category: Large Structures]]
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[[Category: Bingham, R J.]]
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[[Category: Bingham RJ]]
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[[Category: Fairbanks, A J.]]
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[[Category: Fairbanks AJ]]
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[[Category: Ling, Z.]]
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[[Category: Ling Z]]
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[[Category: Moir, J W.B.]]
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[[Category: Moir JWB]]
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[[Category: Suits, M D.L.]]
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[[Category: Suits MDL]]
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[[Category: Taylor, E J.]]
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[[Category: Taylor EJ]]
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[[Category: Acetylglucosaminidase]]
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[[Category: Arthrobacter]]
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[[Category: Carbohydrate binding]]
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[[Category: Family 85]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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Current revision

X-ray crystal structure of the Endo-beta-N-acetylglucosaminidase from Arthrobacter protophormiae E173Q mutant reveals a TIM barrel catalytic domain and two ancillary domains

PDB ID 2vtf

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