Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡ - Wikidata - wikimedia - TriplyDB

Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡

Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡

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The 1.6 Å Crystal Structure of Mycobacterium smegmatis MshC: The Penultimate Enzyme in the Mycothiol Biosynthetic Pathway †Ironing out a new siderophore synthesis strategy The mechanism of domain alternation in the acyl-adenylate forming ligase superfamily member 4-chlorobenzoate: coenzyme A ligase The 2.1 Å crystal structure of an acyl-CoA synthetase from Methanosarcina acetivorans reveals an alternate acyl-binding pocket for small branched acyl substrates Structure of a Eukaryotic Nonribosomal Peptide Synthetase Adenylation Domain That Activates a Large Hydroxamate Amino Acid in Siderophore Biosynthesis Global Conformational Change Associated with the Two-step Reaction Catalyzed by Escherichia coli Lipoate-Protein Ligase A Structure of theD-alanylgriseoluteic acid biosynthetic protein EhpF, an atypical member of the ANL superfamily of adenylating enzymes Crystal Structures of a Populus tomentosa 4-Coumarate:CoA Ligase Shed Light on Its Enzymatic Mechanisms Biochemical and Structural Characterization of Bisubstrate Inhibitors of BasE, the Self-Standing Nonribosomal Peptide Synthetase Adenylate-Forming Enzyme of Acinetobactin Synthesis,Structural and Functional Studies of Fatty Acyl Adenylate Ligases from E. coli and L. pneumophila Defining a Structural and Kinetic Rationale for Paralogous Copies of Phenylacetate-CoA Ligases from the Cystic Fibrosis Pathogen Burkholderia cenocepacia J2315 Structure-Guided Expansion of the Substrate Range of Methylmalonyl Coenzyme A Synthetase (MatB) of Rhodopseudomonas palustris Crystal Structure of Firefly Luciferase in a Second Catalytic Conformation Supports a Domain Alternation Mechanism Structural Basis for Acyl Acceptor Specificity in the Achromobactin Biosynthetic Enzyme AcsD Structural Insights into the Substrate Specificity of the Rhodopseudomonas palustris Protein Acetyltransferase RpPat: IDENTIFICATION OF A LOOP CRITICAL FOR RECOGNITION BY RpPat Structural Basis of the Interaction of MbtH-like Proteins, Putative Regulators of Nonribosomal Peptide Biosynthesis, with Adenylating Enzymes Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains Structure of PA1221, a Nonribosomal Peptide Synthetase Containing Adenylation and Peptidyl Carrier Protein Domains Crystal structures of the first condensation domain of CDA synthetase suggest conformational changes during the synthetic cycle of nonribosomal peptide synthetases.Structure determination of the functional domain interaction of a chimeric nonribosomal peptide synthetase from a challenging crystal with noncrystallographic translational symmetry Domain atrophy creates rare cases of functional partial protein domains Genome scale prediction of substrate specificity for acyl adenylate superfamily of enzymes based on active site residue profiles.Biochemical evidence for conformational changes in the cross-talk between adenylation and peptidyl-carrier protein domains of nonribosomal peptide synthetases.Analysis of the linker region joining the adenylation and carrier protein domains of the modular nonribosomal peptide synthetases.Characterization of an archaeal medium-chain acyl coenzyme A synthetase from Methanosarcina acetivorans Bacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediate The structure of S. lividans acetoacetyl-CoA synthetase shows a novel interaction between the C-terminal extension and the N-terminal domain Determinants within the C-terminal domain of Streptomyces lividans acetyl-CoA synthetase that block acetylation of its active site lysine in vitro by the protein acetyltransferase (Pat) enzyme Stable analogues of OSB-AMP: potent inhibitors of MenE, the o-succinylbenzoate-CoA synthetase from bacterial menaquinone biosynthesis Mechanism of MenE inhibition by acyl-adenylate analogues and discovery of novel antibacterial agents Structural Biology of Nonribosomal Peptide Synthetases Non-ribosomal propeptide precursor in nocardicin A biosynthesis predicted from adenylation domain specificity dependent on the MbtH family protein NocI.Lessons from high-throughput protein crystallization screening: 10 years of practical experience.Adenylating enzymes in Mycobacterium tuberculosis as drug targets.Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.Biochemical characterization and structural insight into aliphatic β-amino acid adenylation enzymes IdnL1 and CmiS6.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Structures of the N-terminal domain of PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP: substrate activation in Pseudomonas Quinolone Signal (PQS) biosynthesis.Structure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity.Complete elucidation of the late steps of bafilomycin biosynthesis in Streptomyces lohii.

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Structural Characterization of a 140° Domain Movement in the Two-Step Reaction Catalyzed by 4-Chlorobenzoate:CoA Ligase † ‡

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2008 nî lūn-bûn

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Andrew M Gulick

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P2860

Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S

Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases

Determination of the MurD mechanism through crystallographic analysis of enzyme complexes

Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1

Domain alternation switches B(12)-dependent methionine synthase to the activation conformation

The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase

Biochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase † , ‡

Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme

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10.1021/BI800696Y

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31

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47

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5230973

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2666193

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