1c7t

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{{Seed}}
 
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[[Image:1c7t.png|left|200px]]
 
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==BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)==
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The line below this paragraph, containing "STRUCTURE_1c7t", creates the "Structure Box" on the page.
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<StructureSection load='1c7t' size='340' side='right'caption='[[1c7t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1c7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C7T FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#8491;</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1c7t| PDB=1c7t | SCENE= }}
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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=1c7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c7t OCA], [https://pdbe.org/1c7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c7t RCSB], [https://www.ebi.ac.uk/pdbsum/1c7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c7t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CHB_SERMA CHB_SERMA] Digests the beta-1,4-glycosidic bonds in N-acetylglucosamine (GlcNAc) oligomers (mainly dimers).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c7/1c7t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1c7t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The catalytic domain of chitobiase (beta-N-1-4 acetylhexosaminidase) from Serratia marcescens, is an alpha/beta TIM-barrel. This enzyme belongs to family 20 of glycosyl hydrolases in which a conserved amino acid pair, aspartate-glutamate, is present (Asp539-Glu540). It was proposed that catalysis by this enzyme family is carried out by glutamate 540 acting as a proton donor and by the acetamido group of the substrate as a nucleophile. We investigated the role of Asp539 and Glu540 by site-directed mutagenesis, biochemical characterization and by structural analyses of chitobiase -substrate co-crystals. We found that both residues are essential for chitobiase activity. The mutations, however, led to subtle changes in the catalytic site. Our results support the model that Glu540 acts as the proton donor and that Asp539 acts in several different ways. Asp539 restrains the acetamido group of the substrate in a specific orientation by forming a hydrogen bond with N2 of the non-reduced (-1) sugar. In addition, this residue participates in substrate binding. It is also required for the correct positioning of Glu540 and may provide additional negative charge at the active site. Thus, these biochemical and structural studies provide a molecular explanation for the functional importance and conservation of these residues.
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===BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)===
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Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.,Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB J Mol Biol. 2000 Jul 14;300(3):611-7. PMID:10884356<ref>PMID:10884356</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1c7t" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10884356}}, adds the Publication Abstract to the page
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10884356 is the PubMed ID number.
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
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{{ABSTRACT_PUBMED_10884356}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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1C7T is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7T OCA].
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</StructureSection>
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:10884356</ref><references group="xtra"/>
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
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[[Category: Oppenheim, A B.]]
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[[Category: Oppenheim AB]]
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[[Category: Papanikolau, Y.]]
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[[Category: Papanikolau Y]]
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[[Category: Petratos, K.]]
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[[Category: Petratos K]]
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[[Category: Prag, G.]]
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[[Category: Prag G]]
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[[Category: Tavlas, G.]]
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[[Category: Tavlas G]]
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[[Category: Vorgias, C E.]]
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[[Category: Vorgias CE]]
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[[Category: Beta-n-acetylhexosaminidase]]
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[[Category: Chitinolysin]]
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[[Category: Co-crystal structure]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Proton donor]]
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[[Category: Site directed mutagenesis]]
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[[Category: X-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:27:53 2009''
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Current revision

BETA-N-ACETYLHEXOSAMINIDASE MUTANT E540D COMPLEXED WITH DI-N ACETYL-D-GLUCOSAMINE (CHITOBIASE)

PDB ID 1c7t

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