CRYSTAL-STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE DNA GYRASE B-PROTEIN

D B  WIGLEY; G J  DAVIES; E J  DODSON; A  MAXWELL; G  DODSON

CRYSTAL-STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE DNA GYRASE B-PROTEIN

D B WIGLEY, G J DAVIES, E J DODSON, A MAXWELL, G DODSON

Chemistry

Research output: Contribution to journal › Article › peer-review

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 angstrom 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 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.

Original language	English
Pages (from-to)	624-629
Number of pages	6
Journal	Nature
Volume	351
Issue number	6328
Publication status	Published - 20 Jun 1991

Keywords

ESCHERICHIA-COLI
A-PROTEIN
GYRB GENE
RESOLUTION
TOPOISOMERASES
REFINEMENT
COMPLEX
SITE

Cite this

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title = "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 angstrom 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 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.",

keywords = "ESCHERICHIA-COLI, A-PROTEIN, GYRB GENE, RESOLUTION, TOPOISOMERASES, REFINEMENT, COMPLEX, SITE",

author = "WIGLEY, {D B} and DAVIES, {G J} and DODSON, {E J} and A MAXWELL and G DODSON",

year = "1991",

month = jun,

day = "20",

language = "English",

volume = "351",

pages = "624--629",

journal = "Nature",

issn = "0028-0836",

publisher = "Nature Publishing Group",

number = "6328",

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TY - JOUR

T1 - CRYSTAL-STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE DNA GYRASE B-PROTEIN

AU - WIGLEY, D B

AU - DAVIES, G J

AU - DODSON, E J

AU - MAXWELL, A

AU - DODSON, G

PY - 1991/6/20

Y1 - 1991/6/20

N2 - 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 angstrom 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 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.

AB - 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 angstrom 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 angstrom hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.

KW - ESCHERICHIA-COLI

KW - A-PROTEIN

KW - GYRB GENE

KW - RESOLUTION

KW - TOPOISOMERASES

KW - REFINEMENT

KW - COMPLEX

KW - SITE

M3 - Article

SN - 0028-0836

VL - 351

SP - 624

EP - 629

JO - Nature

JF - Nature

IS - 6328

ER -