1qba: Difference between revisions
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==BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20== | ==BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20== | ||
<StructureSection load='1qba' size='340' side='right' caption='[[1qba]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1qba' size='340' side='right' caption='[[1qba]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></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=1qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qba OCA], [http://pdbe.org/1qba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qba RCSB], [http://www.ebi.ac.uk/pdbsum/1qba PDBsum]</span></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=1qba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qba OCA], [http://pdbe.org/1qba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qba RCSB], [http://www.ebi.ac.uk/pdbsum/1qba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qba ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/1qba_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qb/1qba_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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1qba" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1qba" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:58, 24 February 2018
BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20BACTERIAL CHITOBIASE, GLYCOSYL HYDROLASE FAMILY 20
Structural highlights
Function[CHB_SERMA] Digests the beta-1,4-glycosidic bonds in N-acetylglucosamine (GlcNAc) oligomers (mainly dimers). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedChitin, 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. 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:8673609[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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