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PDBsum entry 5g3r
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PDB id:
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Hydrolase
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Title:
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Crystal structure of nagz from pseudomonas aeruginosa in complex with n-acetylglucosamine and l-ala-1,6-anhydromurnac
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Structure:
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Beta-hexosaminidase. Chain: a, b. Synonym: beta-n-acetylhexosaminidase,n-acetyl-beta-glucosaminidase. Engineered: yes. Other_details: chain a contains a small fragment (gsh) from the fusion tag used for purification, and chain b contains only a his residue at position -1 from the same fusion tag
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Source:
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Pseudomonas aeruginosa pao1. Organism_taxid: 208964. Strain: pao1. Atcc: 15692. Gene: nagz, pa3005. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.18Å
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R-factor:
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0.197
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R-free:
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0.242
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Authors:
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I.Acebron,C.Artola-Recolons,K.Mahasenan,S.Mobashery,J.A.Hermoso
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Key ref:
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I.Acebrón
et al.
(2017).
Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa.
J Am Chem Soc,
139,
6795-6798.
PubMed id:
DOI:
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Date:
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30-Apr-16
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Release date:
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17-May-17
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PROCHECK
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Headers
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References
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Q9HZK0
(NAGZ_PSEAE) -
Beta-hexosaminidase from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Seq:
Struc:
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332 a.a.
335 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.3.2.1.52
- beta-N-acetylhexosaminidase.
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Reaction:
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Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
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DOI no:
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J Am Chem Soc
139:6795-6798
(2017)
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PubMed id:
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Catalytic Cycle of the N-Acetylglucosaminidase NagZ from Pseudomonas aeruginosa.
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I.Acebrón,
K.V.Mahasenan,
S.De Benedetti,
M.Lee,
C.Artola-Recolons,
D.Hesek,
H.Wang,
J.A.Hermoso,
S.Mobashery.
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ABSTRACT
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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 β-lactam resistance
enzyme, β-lactamase. The enzyme catalyzes hydrolysis of
N-acetyl-β-d-glucosamine-(1→4)-1,6-anhydro-N-acetyl-β-d-muramyl-peptide (1)
to N-acetyl-β-d-glucosamine (2) and 1,6-anhydro-N-acetyl-β-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.
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