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| | <StructureSection load='5g5k' size='340' side='right'caption='[[5g5k]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5g5k' size='340' side='right'caption='[[5g5k]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g5k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5G5K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g5k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G5K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOK:2-ACETAMIDO-1,2-DIDEOXYNOJIRMYCIN'>NOK</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOK:2-ACETAMIDO-1,2-DIDEOXYNOJIRMYCIN'>NOK</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5g5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5k OCA], [http://pdbe.org/5g5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g5k RCSB], [http://www.ebi.ac.uk/pdbsum/5g5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5k ProSAT]</span></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=5g5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g5k OCA], [https://pdbe.org/5g5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g5k RCSB], [https://www.ebi.ac.uk/pdbsum/5g5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g5k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NAGZ_PSEAE NAGZ_PSEAE]] Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.[HAMAP-Rule:MF_00364] | + | [https://www.uniprot.org/uniprot/NAGZ_PSEAE NAGZ_PSEAE] Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.[HAMAP-Rule:MF_00364] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
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| | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | | *[[Beta-Hexosaminidase|Beta-Hexosaminidase]] |
| | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] | | *[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]] |
| | + | *[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-N-acetylhexosaminidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Acebron, I]] | + | [[Category: Acebron I]] |
| - | [[Category: Artola-Recolons, C]] | + | [[Category: Artola-Recolons C]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Hermoso JA]] |
| - | [[Category: Mahasenan, K]] | + | [[Category: Mahasenan K]] |
| - | [[Category: Mobashery, S]] | + | [[Category: Mobashery S]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Beta-hexosaminidase]]
| + | |
| - | [[Category: Cell-wall recycling]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibition]]
| + | |
| - | [[Category: N-acetylglucosaminidase]]
| + | |
| - | [[Category: Peptidoglycan]]
| + | |
| Structural highlights
Function
NAGZ_PSEAE Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.[HAMAP-Rule:MF_00364]
Publication Abstract from PubMed
The N-acetylglucosaminidase NagZ of Pseudomonas aeruginosa catalyzes the first cytoplasmic step in recycling of muropeptides, cell-wall-derived natural products. This reaction regulates gene expression for the beta-lactam resistance enzyme, beta-lactamase. The enzyme catalyzes hydrolysis of N-acetyl-beta-d-glucosamine-(1-->4)-1,6-anhydro-N-acetyl-beta-d-muramyl-peptide (1) to N-acetyl-beta-d-glucosamine (2) and 1,6-anhydro-N-acetyl-beta-d-muramyl-peptide (3). The structural and functional aspects of catalysis by NagZ were investigated by a total of seven X-ray structures, three computational models based on the X-ray structures, molecular-dynamics simulations and mutagenesis. The structural insights came from the unbound state and complexes of NagZ with the substrate, products and a mimetic of the transient oxocarbenium species, which were prepared by synthesis. The mechanism involves a histidine as acid/base catalyst, which is unique for glycosidases. The turnover process utilizes covalent modification of D244, requiring two transition-state species and is regulated by coordination with a zinc ion. The analysis provides a seamless continuum for the catalytic cycle, incorporating large motions by four loops that surround the active site.
Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa.,Acebron I, Mahasenan KV, De Benedetti S, Lee M, Artola-Recolons C, Hesek D, Wang H, Hermoso JA, Mobashery S J Am Chem Soc. 2017 May 10. doi: 10.1021/jacs.7b01626. PMID:28482153[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Acebron I, Mahasenan KV, De Benedetti S, Lee M, Artola-Recolons C, Hesek D, Wang H, Hermoso JA, Mobashery S. Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa. J Am Chem Soc. 2017 May 10. doi: 10.1021/jacs.7b01626. PMID:28482153 doi:http://dx.doi.org/10.1021/jacs.7b01626
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