Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli - Wikidata - wikimedia - TriplyDB

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli

http://www.wikidata.org/entity/Q36760116

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Biochemical and structural characterization of germicidin synthase: analysis of a type III polyketide synthase that employs acyl-ACP as a starter unit donor An ordered water channel in Staphylococcus aureus FabI: unraveling the mechanism of substrate recognition and reduction.Studies ofToxoplasma gondiiandPlasmodium falciparumenoyl acyl carrier protein reductase and implications for the development of antiparasitic agents Structural characterization of CalO2: A putative orsellinic acid P450 oxidase in the calicheamicin biosynthetic pathway Structure of a Specialized Acyl Carrier Protein Essential for Lipid A Biosynthesis with Very Long-Chain Fatty Acids in Open and Closed Conformations High-resolution structures ofThermus thermophilusenoyl-acyl carrier protein reductase in the apo form, in complex with NAD+and in complex with NAD+and triclosan Characterization of Molecular Interactions between ACP and Halogenase Domains in the Curacin A Polyketide Synthase Structure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone Inhibitors Structural and Enzymatic Analyses Reveal the Binding Mode of a Novel Series of Francisella tularensis Enoyl Reductase (FabI) Inhibitors Crystal structures and kinetic properties of enoyl-acyl carrier protein reductase I fromCandidatus Liberibacter asiaticus Crystal structure of hexanoyl-CoA bound to β-ketoacyl reductase FabG4 of Mycobacterium tuberculosis Type II Fatty Acid Synthesis Is Essential for the Replication of Chlamydia trachomatis Structure and reaction mechanism of a novel enone reductase The use of ene adducts to study and engineer enoyl-thioester reductases Using modern tools to probe the structure-function relationship of fatty acid synthases Mechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia mallei The future of crystallography in drug discovery.Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family.Intein-mediated cyclization of bacterial acyl carrier protein stabilizes its folded conformation but does not abolish function.Discovery of a novel and potent class of F. tularensis enoyl-reductase (FabI) inhibitors by molecular shape and electrostatic matching Disrupting the Acyl Carrier Protein/SpoT interaction in vivo: identification of ACP residues involved in the interaction and consequence on growth Molecular recognition between ketosynthase and acyl carrier protein domains of the 6-deoxyerythronolide B synthase.Mechanism and inhibition of the FabI enoyl-ACP reductase from Burkholderia pseudomallei Reversing resistance: The next generation antibacterials.The two functional enoyl-acyl carrier protein reductases of Enterococcus faecalis do not mediate triclosan resistance Diversity in enoyl-acyl carrier protein reductases.Resistance to AFN-1252 arises from missense mutations in Staphylococcus aureus enoyl-acyl carrier protein reductase (FabI).Crystal structure of FabZ-ACP complex reveals a dynamic seesaw-like catalytic mechanism of dehydratase in fatty acid biosynthesis.The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity.Current understanding of fatty acid biosynthesis and the acyl carrier protein.Structure and function of eukaryotic fatty acid synthases.Inhibitors of fatty acid synthesis in prokaryotes and eukaryotes as anti-infective, anticancer and anti-obesity drugs.The structural role of the carrier protein--active controller or passive carrier.The chain-flipping mechanism of ACP (acyl carrier protein)-dependent enzymes appears universal.Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction.Substrate recognition by β-ketoacyl-ACP synthases.Acyl carrier protein structural classification and normal mode analysis.In vitro activities of CG400549, a novel FabI inhibitor, against recently isolated clinical staphylococcal strains in Korea.Molecular dynamics simulations of the Apo-, Holo-, and acyl-forms of Escherichia coli acyl carrier protein.

P2860

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P2860

Structure of acyl carrier protein bound to FabI, the FASII enoyl reductase from Escherichia coli

http://www.wikidata.org/entity/Q36760116

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Structure of acyl carrier prot ...... eductase from Escherichia coli

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Structure of acyl carrier prot ...... eductase from Escherichia coli

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type

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Structure of acyl carrier prot ...... eductase from Escherichia coli

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Structure of acyl carrier prot ...... eductase from Escherichia coli

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Structure of acyl carrier prot ...... eductase from Escherichia coli

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Structure of acyl carrier prot ...... eductase from Escherichia coli

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P1433

Journal of Biological Chemistry

P1476

Structure of acyl carrier prot ...... eductase from Escherichia coli

@en

P2093

Carlos Simmerling

http://www.w3.org/2001/XMLSchema#string

Caroline Kisker

http://www.w3.org/2001/XMLSchema#string

Christopher F Stratton

http://www.w3.org/2001/XMLSchema#string

Peter J Tonge

http://www.w3.org/2001/XMLSchema#string

Polina Novichenok

http://www.w3.org/2001/XMLSchema#string

Richa Rawat

http://www.w3.org/2001/XMLSchema#string

Salma Rafi

http://www.w3.org/2001/XMLSchema#string

Subramaniapillai Kolappan

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Molecular basis of triclosan activity

Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate

Structural basis and mechanism of enoyl reductase inhibition by triclosan

Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan

Molecular basis for triclosan activity involves a flipping loop in the active site

Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites

P304

39285-39293

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scholarly article

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10.1074/JBC.M608758200

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P407

P433

51

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281

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2006-09-29T00:00:00Z

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17012233

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P921

Escherichia coli

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4819000

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