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==E.Coli Gyrase== | |||
---- | ---- | ||
{{STRUCTURE_1ab4| PDB=1ab4 | SCENE=56/568026/Coloured/1}} | {{STRUCTURE_1ab4| PDB=1ab4 | CAPTION=A-subunit (monomer), resolution 2.80Å, 1ab4.pdb| SCENE=56/568026/Coloured/1}} | ||
[[Image:1ab4.png|left|200px]] | [[Image:1ab4.png|left|200px]] | ||
=='''Introduction | ==='''Introduction'''=== | ||
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---- | ---- | ||
=='''Structure'''== | |||
==='''Structure'''=== | |||
[[Image:Gyrasegene.jpg]] | [[Image:Gyrasegene.jpg]] | ||
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There is a '''<scene name='56/568026/Coiledcoil_141819/1'>Coiled-coil</scene> domain''', folowing the tower, with a helical core at the tail region. Two long helices ( | There is a '''<scene name='56/568026/Coiledcoil_141819/1'>Coiled-coil</scene> domain''', folowing the tower, with a helical core at the tail region. Two long helices ( | ||
<scene name='56/568026/Helix14/1'>alpha helix 14</scene> and <scene name='56/568026/Helix18/1'>alpha helix 18</scene>) emanate from this core and connect, together with the C-terminal helix ( | <scene name='56/568026/Helix14/1'>alpha helix 14</scene> and <scene name='56/568026/Helix18/1'>alpha helix 18</scene>) emanate from this core and connect, together with the C-terminal helix (<scene name='56/568026/Helix19/1'>alpha helix 19</scene>), the head and tail fragments. This domain has a small globular domain at it's end and is '''involved in the dimerization creating the <scene name='56/568026/Coiledcoil/1'>C-gate</scene>.''' | ||
<scene name='56/568026/Helix19/1'>alpha helix 19</scene>), the head and tail fragments. This domain has a small globular domain at it's end and is '''involved in the dimerization creating the <scene name='56/568026/Coiledcoil/1'>C-gate</scene>.''' | |||
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---- | ---- | ||
=='''Mechanism'''== | ==='''Mechanism'''=== | ||
40-bp of duplex DNA, the G-segment, bind to the core of the enzyme and are cleaved by the active site tyrosines, while another DNA duplex, the T-segment, is captured through the ATP-induced dimerization of a protein gate, the N-gate. After passage through the transiently broken G-segment (DNA gate), the T-segment exits the protein through another protein gate, the C-gate. ATP hydrolysis and release reset the conformation of the enzyme and DNA to their initial state, poised for another strand-passage event or release of the DNA. | 40-bp of duplex DNA, the G-segment, bind to the core of the enzyme and are cleaved by the active site tyrosines, while another DNA duplex, the T-segment, is captured through the ATP-induced dimerization of a protein gate, the N-gate. After passage through the transiently broken G-segment (DNA gate), the T-segment exits the protein through another protein gate, the C-gate. ATP hydrolysis and release reset the conformation of the enzyme and DNA to their initial state, poised for another strand-passage event or release of the DNA. | ||
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---- | ---- | ||
=='''Reaction'''== | ==='''Reaction'''=== | ||
The process of DNA supercoiling by gyrase is the following : | The process of DNA supercoiling by gyrase is the following : | ||
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There are also others antibiotics, like the Cinodine which binds DNA and inhibits its supercoiling by gyrase. | There are also others antibiotics, like the Cinodine which binds DNA and inhibits its supercoiling by gyrase. | ||
==See Also== | ===See Also=== | ||
*[[Gyrase|Gyrase]] | *[[Gyrase|Gyrase]] | ||
*[[Topoisomerase|Topoisomerase]] | *[[Topoisomerase|Topoisomerase]] | ||
== | ===References=== | ||
<ref group="xtra">PMID:009278055</ref><references group="xtra"/> | <ref group="xtra">PMID:009278055</ref><references group="xtra"/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Topoisomerase ii]] | [[Category: Topoisomerase ii]] | ||
*Reece, Richard J., Anthony Maxwell, and James C. Wang. "DNA gyrase: structure and function." Critical reviews in biochemistry and molecular biology 26.3-4 (1991): 335-375. | *Reece, Richard J., Anthony Maxwell, and James C. Wang. "DNA gyrase: structure and function." Critical reviews in biochemistry and molecular biology 26.3-4 (1991): 335-375. | ||
*Nicole M. Baker, Steven Weigand, Sarah Maar-Mathiasand Alfonso Mondrago´n "Solution structures of DNA-bound gyrase" Nucleic Acids Res. 2011 January; 39(2): 755–766. | |||
