The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism (Q24685438)

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Language	Label	Description	Also known as
English	The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism	scientific article

Statements

instance of

scholarly article

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title

The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism (English)

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main subject

crystal structure

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chloramphenicol

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based on heuristic

inferred from title

author name string

T Izard

series ordinal

1

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J Ellis

series ordinal

2

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language of work or name

English

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publication date

1 June 2000

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published in

The EMBO Journal

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volume

19

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issue

11

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page(s)

2690-700

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cites work

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Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+

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Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24)

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Domain movements in protein kinases

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Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer

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Chloramphenicol acetyltransferase

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High‐resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer

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Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer

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Chloramphenicol acetylation in Streptomyces

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Cubic crystals of chloramphenicol phosphotransferase fromStreptomyces venezuelaein complex with chloramphenicol

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Bayesian weighting for macromolecular crystallographic refinement

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

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based on heuristic

inferred from PubMed ID database lookup

Induced-fit movements in adenylate kinases

1 reference

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PubMed

reference URL

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12 December 2020

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inferred from PubMed ID database lookup

Processing of X-ray diffraction data collected in oscillation mode

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Phosphotransferase sequence homology

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Nitrogen metabolism and chloramphenicol production in Streptomyces venezuelae

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein kinases

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

New structure--novel fold?

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The three-dimensional structure of shikimate kinase

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/10835366

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1093/EMBOJ/19.11.2690

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1066414

OpenCitations bibliographic resource ID

1066414

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1066414

PMC publication ID

212772

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1066414

PubMed publication ID

10835366

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1066414

ResearchGate publication ID

12483577

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