Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions (Q27681358)

ORCID Public Data File 2021

author name string

Javier M González

1

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María-Rocío Meini

2

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Pablo E Tomatis

3

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Francisco J Medrano Martín

4

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Julia A Cricco

5

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Alejandro J Vila

Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases

6

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publication date

August 2012

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published in

Nature Chemical Biology

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volume

8

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issue

8

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page(s)

698-700

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cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

20 March 2017

1 reference

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The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

20 March 2017

1 reference

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Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis

20 March 2017

1 reference

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Coordination chemistry of bacterial metal transport and sensing

7 April 2017

1 reference

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Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3470787

A place for thioether chemistry in cellular copper ion recognition and trafficking

29 September 2017

1 reference

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Metallo-beta-lactamases: novel weaponry for antibiotic resistance in bacteria

29 September 2017

1 reference

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Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity

29 September 2017

1 reference

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Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold

29 September 2017

1 reference

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Functional analysis of the active site of a metallo-beta-lactamase proliferating in Japan

29 September 2017

1 reference

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Spectroscopic characterization of a binuclear metal site in Bacillus cereus beta-lactamase II.

29 September 2017

1 reference

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Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

2 June 2018

1 reference

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Crystal Structure of Pseudomonas aeruginosa SPM-1 Provides Insights into Variable Zinc Affinity of Metallo-β-lactamases

21 January 2018

1 reference

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Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.1005

Positively Cooperative Binding of Zinc Ions to Bacillus cereus 569/H/9 β-Lactamase II Suggests that the Binuclear Enzyme Is the Only Relevant Form for Catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNCHEMBIO.1005

Enzyme Deactivation Due to Metal-Ion Dissociation during Turnover of the Cobalt-β-Lactamase Catalyzed Hydrolysis of β-Lactams†

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22729148

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Evidence for a dinuclear active site in the metallo-beta-lactamase BcII with substoichiometric Co(II). A new model for metal uptake

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22729148

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Metal content and localization during turnover in B. cereus metallo-beta-lactamase

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22729148

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NCHEMBIO.1005

1 reference

Dimensions Publication ID

4391873

1003226600

0 references

4391873

1 reference

1 reference

1 reference