Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity (Q27685295)

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English	Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity	scientific article

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scholarly article

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Structure of arylamine N-acetyltransferase from Mycobacterium tuberculosis determined by cross-seeding with the homologous protein from M. marinum: triumph over adversity (English)

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Mycobacterium tuberculosis

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Mycobacterium marinum

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protein structure

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Areej Abuhammad

object named as

Areej Abuhammad

1

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object named as

Elspeth F Garman

7

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Michael A McDonough

object named as

Michael A McDonough

3

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6

object named as

Edith Sim

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author name string

Edward D Lowe

2

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Patrick D Shaw Stewart

4

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Stefan A Kolek

5

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publication date

August 2013

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Acta Crystallographica Section D: Biological Crystallography

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69

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Pt 8

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1433-46

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Piperidinols That Show Anti-Tubercular Activity as Inhibitors of Arylamine N-Acetyltransferase: An Essential Enzyme for Mycobacterial Survival Inside Macrophages

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Improvement of the expression and purification of Mycobacterium tuberculosis arylamine N-acetyltransferase (TBNAT) a potential target for novel anti-tubercular agents

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21 January 2018

Probing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active site

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21 January 2018

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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The potential of azole antifungals against latent/persistent tuberculosis

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Characterization of the putative operon containing arylamine N-acetyltransferase (nat) in Mycobacterium bovis BCG.

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A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis

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The potential impact of structural genomics on tuberculosis drug discovery

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21 January 2018

Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors

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21 January 2018

Arylamine N-acetyltransferase is required for synthesis of mycolic acids and complex lipids in Mycobacterium bovis BCG and represents a novel drug target

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Strength of NH···S Hydrogen Bonds in Methionine Residues Revealed by Gas-Phase IR/UV Spectroscopy.

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Structural and functional studies of mycobacterial IspD enzymes

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An approach to identifying novel substrates of bacterial arylamine N-acetyltransferases

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

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MolProbity: all-atom structure validation for macromolecular crystallography

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Crystal structure of Ski8p, a WD-repeat protein with dual roles in mRNA metabolism and meiotic recombination

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The TB Structural Genomics Consortium: a decade of progress

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21 January 2018

Advances in Mycobacterium tuberculosis structural genomics: investigating potential chinks in the armor of a deadly pathogen

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21 January 2018

New tuberculosis drugs on the horizon

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Rational design of protein stability: effect of (2S,4R)-4-fluoroproline on the stability and folding pathway of ubiquitin

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Dominant forces in protein folding

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A flavin-dependent monooxygenase from Mycobacterium tuberculosis involved in cholesterol catabolism

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Features and development of Coot

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Thermofluor-based high-throughput stability optimization of proteins for structural studies

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Nontuberculous mycobacteria in the environment

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21 January 2018

Analysis of β-amino alcohols as inhibitors of the potential anti-tubercular target N-acetyltransferase

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21 January 2018

Comparison of the Arylamine N-acetyltransferase from Mycobacterium marinum and Mycobacterium tuberculosis.

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21 January 2018

Design, synthesis and structure-activity relationships of 3,5-diaryl-1H-pyrazoles as inhibitors of arylamine N-acetyltransferase

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Divergence of cofactor recognition across evolution: coenzyme A binding in a prokaryotic arylamine N-acetyltransferase

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The TB Alliance: overcoming challenges to chart the future course of TB drug development

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Cholesterol catabolism by Mycobacterium tuberculosis requires transcriptional and metabolic adaptations

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New drugs for the treatment of tuberculosis: hope and reality

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Structure of Mesorhizobium loti arylamine N-acetyltransferase 1.

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Arabinogalactan and lipoarabinomannan biosynthesis: structure, biogenesis and their potential as drug targets.

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Unbiased binding assays for discovering small-molecule probes and drugs

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Cholesterol utilization in mycobacteria is controlled by two TetR-type transcriptional regulators: kstR and kstR2

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Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis

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Structure of HsaD, a steroid-degrading hydrolase, fromMycobacterium tuberculosis

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Characterization of a Carbon-Carbon Hydrolase from Mycobacterium tuberculosis Involved in Cholesterol Metabolism

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Small molecule colorimetric probes for specific detection of human arylamine N-acetyltransferase 1, a potential breast cancer biomarker

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High-throughput thermal scanning: a general, rapid dye-binding thermal shift screen for protein engineering

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Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis

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Functional and structural characterization of the arylamine N-acetyltransferase from the opportunistic pathogen Nocardia farcinica

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Phasercrystallographic software

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High throughput crystallography of TB drug targets.

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The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

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Shape complementarity at protein-protein interfaces

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Cholesterol catabolism as a therapeutic target in Mycobacterium tuberculosis

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Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p

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Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data.

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The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid

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Genes required for mycobacterial growth defined by high density mutagenesis

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Extensively drug-resistant tuberculosis: a new face to an old pathogen.

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Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis

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Arylamine N-acetyltransferases--from drug metabolism and pharmacogenetics to identification of novel targets for pharmacological intervention

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Arylamine N-acetyltransferases in mycobacteria

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Structure of arylamine N-acetyltransferase reveals a catalytic triad

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The Global Plan to Stop TB: a unique opportunity to address poverty and the Millennium Development Goals

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The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology.

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Totally drug-resistant tuberculosis in India.

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Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

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Computational and experimental analyses of mammalian arylamine N-acetyltransferase structure and function

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Arylamine N-acetyltransferase from fast (C57BL6) and slow (A/J) N-acetylating strains of mice

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Identification of arylamine N-acetyltransferase inhibitors as an approach towards novel anti-tuberculars

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21 January 2018

Structure and mechanism of arylamine N-acetyltransferases.

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Novel small-molecule inhibitors of arylamine N-acetyltransferases: drug discovery by high-throughput screening.

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Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases

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Hydrogen bonds and salt bridges across protein-protein interfaces

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Studies of a ring-cleaving dioxygenase illuminate the role of cholesterol metabolism in the pathogenesis of Mycobacterium tuberculosis

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The magic bullets and tuberculosis drug targets.

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10.1107/S0907444913015126

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