1991
DOI: 10.1038/351624a0
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Crystal structure of an N-terminal fragment of the DNA gyrase B protein

Abstract: The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 A resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 A hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.

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Cited by 535 publications
(617 citation statements)
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“…Although nucleotide binding to the fusion protein could not be detected, the predicted amino acid sequence of VirB11 contains a conserved sequence (GPTGSGKT) which corresponds to the Walker box A nucleotide-binding site (GxxGxGKT/S) in many ATP-binding proteins (63). The amino acids of this conserved region have been shown to be important for binding nucleotides in these proteins by nuclear magnetic resonance (17)(18)(19), X-ray crystallography (24,55,69), and genetic (23,49,60) studies. The highly conserved lysine is thought to function by interacting with the ␥-phosphate of ATP (17-19, 55, 69), and changes at this position greatly reduce nucleotide binding (5,23,46,48,52,60).…”
Section: Resultsmentioning
confidence: 99%
“…Although nucleotide binding to the fusion protein could not be detected, the predicted amino acid sequence of VirB11 contains a conserved sequence (GPTGSGKT) which corresponds to the Walker box A nucleotide-binding site (GxxGxGKT/S) in many ATP-binding proteins (63). The amino acids of this conserved region have been shown to be important for binding nucleotides in these proteins by nuclear magnetic resonance (17)(18)(19), X-ray crystallography (24,55,69), and genetic (23,49,60) studies. The highly conserved lysine is thought to function by interacting with the ␥-phosphate of ATP (17-19, 55, 69), and changes at this position greatly reduce nucleotide binding (5,23,46,48,52,60).…”
Section: Resultsmentioning
confidence: 99%
“…For example, the remodeling of strand 1 and the "lid" helix in response to ligand is a prominent feature of the transition between the ADP-and ATP-bound forms of both MutL (20,38) and DNA gyrase (19,39). Although the lid elements, the helix 1-4-5 subdomain, in GRP94 open in response to ATP/ADP binding rather than close as they do in MutL and DNA gyrase, the conformational change between the open and closed forms of GRP94 may functionally correlate to the switch between the activated and inactive forms of MutL and DNA gyrase.…”
Section: Discussionmentioning
confidence: 99%
“…The detection of ligand-dependent conformational changes has been instrumental in the development of mechanistic models for DNA gyrase and MutL action (19,20,38,39), and GRP94 exhibits many of these same conformational changes. For example, the remodeling of strand 1 and the "lid" helix in response to ligand is a prominent feature of the transition between the ADP-and ATP-bound forms of both MutL (20,38) and DNA gyrase (19,39).…”
Section: Discussionmentioning
confidence: 99%
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“…In this model, a free or DNA-bound enzyme is assumed to have two major conformations: a closed-clamp form when ATP or its nonhydrolysable b , -imido analogue AMPPNP is bound to the enzyme, and an open-clamp form in the absence of bound nucleotide. The closed or open state of the protein clamp is dependent on the formation of contacts between the amino-terminal domains of the pair of polypeptides of the dimeric enzyme (Wigley et al 1991). A second DNA segment can enter a DNAbound enzyme only if the enzyme is in the open-clamp state.…”
Section: Introductionmentioning
confidence: 99%