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| | <StructureSection load='4qdn' size='340' side='right'caption='[[4qdn]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4qdn' size='340' side='right'caption='[[4qdn]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qdn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QDN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qdn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QDN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THEMA_01495, TM0633, Tmari_0634, TM_0633 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=4qdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qdn OCA], [https://pdbe.org/4qdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qdn RCSB], [https://www.ebi.ac.uk/pdbsum/4qdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qdn ProSAT]</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=4qdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qdn OCA], [http://pdbe.org/4qdn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qdn RCSB], [http://www.ebi.ac.uk/pdbsum/4qdn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qdn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9WZA1_THEMA Q9WZA1_THEMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4qdn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4qdn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thema]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Bourne, Y]] | + | [[Category: Bourne Y]] |
| - | [[Category: Lipski, A]] | + | [[Category: Lipski A]] |
| - | [[Category: Nurizzo, D]] | + | [[Category: Nurizzo D]] |
| - | [[Category: Vincent, F]] | + | [[Category: Vincent F]] |
| - | [[Category: Bacterial peptidoglycan hydrolysis]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inverting mechanism]]
| + | |
| - | [[Category: Typical lysozyme alpha-beta fold with only the alpha-lobe]]
| + | |
| Structural highlights
Function
Q9WZA1_THEMA
Publication Abstract from PubMed
Members of the GH73 glycosidase family cleave the beta-1,4-glycosidic bond between the N-acetylglucosaminyl (GlcNAc) and N-acetylmuramyl (MurNAc) moieties in bacterial peptidoglycan. A catalytic mechanism has been proposed for members FlgJ, Auto, AcmA and Atl(WM) and the structural analysis of FlgJ and Auto revealed a conserved alpha/beta fold reminiscent of the distantly-related GH23 lysozyme. Comparison of the active site residues reveals variability in the nature of the catalytic general base suggesting two distinct catalytic mechanisms: an inverting mechanism involving two distant glutamate residues and a substrate-assisted mechanism involving anchimeric assistance by the C2-acetamido group of the GlcNAc moiety. Herein, we present the biochemical characterization and crystal structure of TM0633 from the hyperthermophilic bacterium Thermotoga maritima. TM0633 adopts the alpha/beta fold of the family and displays beta-N-acetylglucosaminidase activity on intact peptidoglycan sacculi. Site-directed mutagenesis identifies Glu34, Glu65 and Tyr118 as important residues for catalysis. A thorough bioinformatic analysis of the GH73 sequences identified five phylogenetic clusters. TM0633, FlgJ and Auto belong to a group of three clusters that conserve two carboxylate residues involved in a classical inverting acid-base mechanism. Members of the other two clusters lack a conserved catalytic general base supporting a substrate-assisted mechanism. Molecular modeling of representative members from each cluster suggests that variability in length of the beta-hairpin region above the active site confers ligand binding specificity and modulates the catalytic mechanisms within the GH73 family.
Structural and biochemical characterization of the beta-N-acetylglucosaminidase from Thermotoga maritima: toward rationalization of mechanistic knowledge in the GH73 family.,Lipski A, Herve M, Lombard V, Nurizzo D, Mengin-Lecreulx D, Bourne Y, Vincent F Glycobiology. 2014 Oct 24. pii: cwu113. PMID:25344445[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lipski A, Herve M, Lombard V, Nurizzo D, Mengin-Lecreulx D, Bourne Y, Vincent F. Structural and biochemical characterization of the beta-N-acetylglucosaminidase from Thermotoga maritima: toward rationalization of mechanistic knowledge in the GH73 family. Glycobiology. 2014 Oct 24. pii: cwu113. PMID:25344445 doi:http://dx.doi.org/10.1093/glycob/cwu113
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