(Q27641496)

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Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase

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Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase (English)

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Pseudomonas aeruginosa

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Streptococcus pneumoniae

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based on heuristic

inferred from title

Staphylococcus aureus

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based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

Thermotoga maritima

object named as

Thermotoga maritima

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based on heuristic

inferred from title

Daniel McMullan

5

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2

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Andreas Kreusch

1

object named as

Andreas Kreusch

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4

object named as

Heath Klock

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7

object named as

Tanya Shin

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11

object named as

Scott A Lesley

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author name string

Chris C Lee

3

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Ken Ng

6

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Juli Vincent

8

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Ian Warner

9

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Christer Ericson

10

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language of work or name

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publication date

4 July 2003

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Journal of Molecular Biology

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330

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2

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309-21

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Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase

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Peptide deformylase in Staphylococcus aureus: resistance to inhibition is mediated by mutations in the formyltransferase gene

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Deformylase as a novel antibacterial target.

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Peptide deformylase as a target for new generation, broad spectrum antimicrobial agents

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On the release of the formyl group from nascent protein

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Methionine aminopeptidase gene of Escherichia coli is essential for cell growth

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Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli.

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Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms

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Peptide deformylase of eukaryotic protists: a target for new antiparasitic agents?

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Crystal structure of the Escherichia coli peptide deformylase

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Iron center, substrate recognition and mechanism of peptide deformylase

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The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents

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Crystal structure of type II peptide deformylase from Staphylococcus aureus

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Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design

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Oxygen-mediated inactivation of peptide deformylase

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Antibiotic Activity and Characterization of BB-3497, a Novel Peptide Deformylase Inhibitor

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Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site

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Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133.

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Control of peptide deformylase activity by metal cations

1 reference

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Mechanism of chalcone synthase. pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase.

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Thiol proteases

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Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers

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Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation

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Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis

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Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms

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Geometry of metal-ligand interactions in proteins

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The C-terminal domain of peptide deformylase is disordered and dispensable for activity

1 reference

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Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion.

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Structural basis for the design of antibiotics targeting peptide deformylase

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Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline

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Formate dehydrogenase-coupled spectrophotometric assay of peptide deformylase

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10.1016/S0022-2836(03)00596-5

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