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Structure and functions of the GNAT superfamily of acetyltransferases.
TLDR
This review of the Gcn5-related N-acetyltransferases will examine those members of this superfamily that have been both structurally and mechanistically characterized. Expand
A Fluoroquinolone Resistance Protein from Mycobacterium tuberculosis That Mimics DNA
TLDR
Its three-dimensional structure reveals a fold, which is named the right-handed quadrilateral β helix, that exhibits size, shape, and electrostatic similarity to B-form DNA and explains both its inhibitory effect on DNA gyrase and fluoroquinolone resistance resulting from the protein's expression in vivo. Expand
Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum
TLDR
Molecular models of the ternary complex suggest a mechanism in which the β-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1-l-myo-inositol-1- phosphate while at the same time promoting the cleavage of the sugar nucleotide bond. Expand
Structure of human phosphatidylcholine transfer protein in complex with its ligand
TLDR
The structures presented here provide a basis for rationalizing the specificity of PC-TP for PtdCho and may identify common features used by START proteins to bind their hydrophobic ligand-binding proteins. Expand
Pentapeptide repeat proteins.
TLDR
The three-dimensional structure of the first member of the PRP family was determined for the fluoroquinolone resistance protein (MfpA) from Mycobacterium tuberculosis and revealed that the pentapeptide repeats encode the folding of a novel right-handed quadrilateral beta-helix. Expand
Structure of Acinetobacter strain ADP1 protocatechuate 3, 4-dioxygenase at 2.2 A resolution: implications for the mechanism of an intradiol dioxygenase.
TLDR
The structure of the 4-NC complex supports the view that resonance delocalization of the positive character of the nitrogen prevents substrate activation and confirms previous work that protocatechuate 3,4-dioxygenases have three coordination sites available for binding by exogenous substrates. Expand
Structure of QnrB1, a Plasmid-mediated Fluoroquinolone Resistance Factor*
TLDR
A mechanism in which PRP-topoisomerase poison resistance factors bind to and disrupt the quinolone-DNA-gyrase interaction is proposed. Expand
Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates
TLDR
A structural analysis of the crystal structure of the AAC(2′)-Ic from Mycobacterium tuberculosis suggests that the enzyme may acetylate a key biosynthetic intermediate of mycothiol, the major reducing agent in mycobacteria, and participate in the regulation of cellular redox potential. Expand
Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for Nα‐acetylation of ribosomal protein S18
TLDR
The RimIST‐bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis. Expand
The Active Site of O-Acetylserine Sulfhydrylase Is the Anchor Point for Bienzyme Complex Formation with Serine Acetyltransferase
TLDR
The crystal structure of OASS in complex with a C-terminal peptide of SAT required for bienzyme complex formation is determined, explaining the partial inhibition of Oass by SAT on complex formation as well as the competitive dissociation of the complex by O-acetylserine. Expand
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