Nucleotide Binding to the 43-Kilodalton N-Terminal Fragment of the DNA Gyrase B Protein

Biochemistry ◽  
1995 ◽  
Vol 34 (30) ◽  
pp. 9801-9808 ◽  
Author(s):  
Janid A. Ali ◽  
George Orphanides ◽  
Anthony Maxwell
Keyword(s):  
Dna Gyrase ◽  
Nucleotide Binding ◽  
Terminal Fragment

Crystal structure of an N-terminal fragment of the DNA gyrase B protein

Nature ◽  
1991 ◽  
Vol 351 (6328) ◽  
pp. 624-629 ◽  
Author(s):  
Dale B. Wigley ◽  
Gideon J. Davies ◽  
Eleanor J. Dodson ◽  
Anthony Maxwell ◽  
Guy Dodson
Keyword(s):  
Crystal Structure ◽  
Dna Gyrase ◽  
Terminal Fragment

The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs

Biochemistry ◽  
1993 ◽  
Vol 32 (10) ◽  
pp. 2717-2724 ◽  
Author(s):  
Janid A. Ali ◽  
Andrew P. Jackson ◽  
Alison J. Howells ◽  
Anthony Maxwell
Keyword(s):  
Dna Gyrase ◽  
Terminal Fragment ◽  
Coumarin Drugs

scholarly journals Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase

2004 ◽  
Vol 48 (5) ◽  
pp. 1856-1864 ◽  
Author(s):  
Steven Bellon ◽  
Jonathan D. Parsons ◽  
Yunyi Wei ◽  
Koto Hayakawa ◽  
Lora L. Swenson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Atp Hydrolysis ◽  
Bacterial Genome ◽  
Catalytic Efficiency ◽  
Dna Gyrase ◽  
Substrate Affinity ◽  
Topoisomerase Iv ◽  
Terminal Fragment ◽  
Essential Function

ABSTRACT Topoisomerase IV and DNA gyrase are related bacterial type II topoisomerases that utilize the free energy from ATP hydrolysis to catalyze topological changes in the bacterial genome. The essential function of DNA gyrase is the introduction of negative DNA supercoils into the genome, whereas the essential function of topoisomerase IV is to decatenate daughter chromosomes following replication. Here, we report the crystal structures of a 43-kDa N-terminal fragment of Escherichia coli topoisomerase IV ParE subunit complexed with adenylyl-imidodiphosphate at 2.0-Å resolution and a 24-kDa N-terminal fragment of the ParE subunit complexed with novobiocin at 2.1-Å resolution. The solved ParE structures are strikingly similar to the known gyrase B (GyrB) subunit structures. We also identified single-position equivalent amino acid residues in ParE (M74) and in GyrB (I78) that, when exchanged, increased the potency of novobiocin against topoisomerase IV by nearly 20-fold (to 12 nM). The corresponding exchange in gyrase (I78 M) yielded a 20-fold decrease in the potency of novobiocin (to 1.0 μM). These data offer an explanation for the observation that novobiocin is significantly less potent against topoisomerase IV than against DNA gyrase. Additionally, the enzyme kinetic parameters were affected. In gyrase, the ATP Km increased ≈5-fold and the V max decreased ≈30%. In contrast, the topoisomerase IV ATP Km decreased by a factor of 6, and the V max increased ≈2-fold from the wild-type values. These data demonstrate that the ParE M74 and GyrB I78 side chains impart opposite effects on the enzyme's substrate affinity and catalytic efficiency.

Nucleotide Binding to DNA Gyrase Causes Loss of DNA Wrap

2004 ◽  
Vol 337 (3) ◽  
pp. 597-610 ◽  
Author(s):  
Jonathan G. Heddle ◽  
Sylvain Mitelheiser ◽  
Anthony Maxwell ◽  
Neil H. Thomson
Keyword(s):  
Dna Gyrase ◽  
Nucleotide Binding

scholarly journals Mode of action of GR122222X, a novel inhibitor of bacterial DNA gyrase.

1996 ◽  
Vol 40 (2) ◽  
pp. 473-476 ◽  
Author(s):  
M Oram ◽  
B Dosanjh ◽  
N A Gormley ◽  
C V Smith ◽  
L M Fisher ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Mode Of Action ◽  
Potent Inhibitor ◽  
Dna Gyrase ◽  
Bacterial Dna ◽  
B Subunit ◽  
Terminal Fragment

GR122222X is a potent inhibitor of the supercoiling reaction of bacterial DNA gyrase. We show that this compound binds stoichiometrically to inactivate the ATPase activity of a 43-kDa N-terminal fragment of the B subunit and competitively inhibits the binding of a radiolabelled coumarin drug to N-terminal fragments of GyrB. These and other data suggest that GR122222X has a mode of action similar, but not identical, to that of coumarin antibiotics.

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