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1qba

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[[Image:1qba.gif|left|200px]]
 
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==BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20==
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The line below this paragraph, containing "STRUCTURE_1qba", creates the "Structure Box" on the page.
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<StructureSection load='1qba' size='340' side='right'caption='[[1qba]], [[Resolution|resolution]] 1.85&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'>[[1qba]] 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=1QBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QBA 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]] 1.85&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1qba| PDB=1qba | 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=1qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qba OCA], [https://pdbe.org/1qba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qba RCSB], [https://www.ebi.ac.uk/pdbsum/1qba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qba 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/qb/1qba_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1qba ConSurf].
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<div style="clear:both"></div>
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'''BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20'''
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==See Also==
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*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
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*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
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==Overview==
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__TOC__
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Chitin, the second most abundant polysaccharide on earth, is degraded by chitinases and chitobiases. The structure of Serratia marcescens chitobiase has been refined at 1.9 A resolution. The mature protein is folded into four domains and its active site is situated at the C-terminal end of the central (beta alpha)8-barrel. Based on the structure of the complex with the substrate disaccharide chitobiose, we propose an acid-base reaction mechanism, in which only one protein carboxylate acts as catalytic acid, while the nucleophile is the polar acetamido group of the sugar in a substrate-assisted reaction. The structural data lead to the hypothesis that the reaction proceeds with retention of anomeric configuration. The structure allows us to model the catalytic domain of the homologous hexosaminidases to give a structural rationale to pathogenic mutations that underlie Tay-Sachs and Sandhoff disease.
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</StructureSection>
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[[Category: Large Structures]]
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==About this Structure==
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1QBA is a [[Single protein]] 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=1QBA OCA].
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==Reference==
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Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease., Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE, Nat Struct Biol. 1996 Jul;3(7):638-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8673609 8673609]
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[[Category: Beta-N-acetylhexosaminidase]]
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
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[[Category: Single protein]]
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[[Category: Dauter Z]]
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[[Category: Dauter, Z.]]
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[[Category: Oppenheim A]]
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[[Category: Oppenheim, A.]]
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[[Category: Perrakis A]]
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[[Category: Perrakis, A.]]
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[[Category: Tews I]]
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[[Category: Tews, I.]]
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[[Category: Vorgias CE]]
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[[Category: Vorgias, C E.]]
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[[Category: Wilson KS]]
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[[Category: Wilson, K S.]]
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[[Category: Ba8-barrel]]
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[[Category: Chitinolysis]]
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[[Category: Chitobiase]]
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[[Category: Glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:47 2008''
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Current revision

BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20

PDB ID 1qba

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