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Record W2144167312 · doi:10.1074/jbc.m114.611400

Structural Basis for the De-N-acetylation of Poly-β-1,6-N-acetyl-d-glucosamine in Gram-positive Bacteria

2014· article· en· W2144167312 on OpenAlexafffund
Dustin J. Little, Natalie C. Bamford, Varvara Pokrovskaya, Howard Robinson, Mark Nitz, P. Lynne Howell

Bibliographic record

VenueJournal of Biological Chemistry · 2014
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicBiopolymer Synthesis and Applications
Canadian institutionsHospital for Sick ChildrenUniversity of Toronto
FundersNational Institute of General Medical SciencesBiological and Environmental ResearchNatural Sciences and Engineering Research Council of CanadaNational Institutes of HealthCanadian Institutes of Health ResearchNational Institute of Biomedical Imaging and BioengineeringHospital for Sick ChildrenUniversity of TorontoU.S. Department of Energy
KeywordsGlucosamineAcetylationD-GlucosamineBacteriaChemistryBiochemistryStereochemistryMicrobiologyBiologyGenetics

Abstract

fetched live from OpenAlex

Exopolysaccharides are required for the development and integrity of biofilms produced by a wide variety of bacteria. In staphylococci, partial de- N -acetylation of the exopolysaccharide poly-β-1,6- N -acetyl-d-glucosamine (PNAG) by the extracellular protein IcaB is required for biofilm formation. To understand the molecular basis for PNAG de- N -acetylation, the structure of IcaB from Ammonifex degensii (IcaB Ad ) has been determined to 1.7 Å resolution. The structure of IcaB Ad reveals a (β/α) 7 barrel common to the family four carbohydrate esterases (CE4s) with the canonical motifs circularly permuted. The metal dependence of IcaB Ad is similar to most CE4s showing the maximum rates of de- N -acetylation with Ni 2+ , Co 2+ , and Zn 2+ . From docking studies with β-1,6-GlcNAc oligomers and structural comparison to PgaB from Escherichia coli , the Gram-negative homologue of IcaB, we identify Arg-45, Tyr-67, and Trp-180 as key residues for PNAG binding during catalysis. The absence of these residues in PgaB provides a rationale for the requirement of a C-terminal domain for efficient deacetylation of PNAG in Gram-negative species. Mutational analysis of conserved active site residues suggests that IcaB uses an altered catalytic mechanism in comparison to other characterized CE4 members. Furthermore, we identified a conserved surface-exposed hydrophobic loop found only in Gram-positive homologues of IcaB. Our data suggest that this loop is required for membrane association and likely anchors IcaB to the membrane during polysaccharide biosynthesis. The work presented herein will help guide the design of IcaB inhibitors to combat biofilm formation by staphylococci.IcaB is a poly-β-1,6- N -acetyl-d-glucosamine (PNAG) deacetylase required for polysaccharide intercellular adhesion-dependent biofilm formation by staphylococci. Results The structure of Ammonifex degensii IcaB has been determined and its catalytic mechanism and localization characterized. Conclusion IcaB is a membrane-associated PNAG deacetylase that uses an altered catalytic mechanism relative to other family 4 carbohydrate esterases. Significance First structural characterization of a Gram-positive PNAG deacetylase.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.003

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.015
GPT teacher head0.257
Teacher spread0.242 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations33
Published2014
Admission routes2
Has abstractyes

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