1zi0

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|SITE=
|SITE=
|LIGAND=
|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] </span>
|GENE= gyrA, hisW, nalA, parD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= gyrA, hisW, nalA, parD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zi0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zi0 OCA], [http://www.ebi.ac.uk/pdbsum/1zi0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zi0 RCSB]</span>
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[[Category: Ruthenburg, A J.]]
[[Category: Ruthenburg, A J.]]
[[Category: Verdine, G L.]]
[[Category: Verdine, G L.]]
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[[Category: beta pinwheel; gyrase; topoisomerase; spiralling beta pinwheel; dna wrapping]]
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[[Category: beta pinwheel]]
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[[Category: dna wrapping]]
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[[Category: gyrase]]
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[[Category: spiralling beta pinwheel]]
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[[Category: topoisomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:36:53 2008''

Revision as of 22:36, 30 March 2008


PDB ID 1zi0

Drag the structure with the mouse to rotate
, resolution 2.60Å
Gene: gyrA, hisW, nalA, parD (Escherichia coli)
Activity: DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



A Superhelical Spiral in Escherichia coli DNA Gyrase A C-terminal Domain Imparts Unidirectional Supercoiling Bias


Overview

DNA gyrase is unique among type II topoisomerases in that its DNA supercoiling activity is unidirectional. The C-terminal domain of the gyrase A subunit (GyrA-CTD) is required for this supercoiling bias. We report here the x-ray structure of the Escherichia coli GyrA-CTD (Protein Data Bank code 1ZI0). The E. coli GyrA-CTD adopts a circular-shaped beta-pinwheel fold first seen in the Borrelia burgdorferi GyrA-CTD. However, whereas the B. burgdorferi GyrA-CTD is flat, the E. coli GyrA-CTD is spiral. DNA relaxation assays reveal that the E. coli GyrA-CTD wraps DNA inducing substantial (+) superhelicity, while the B. burgdorferi GyrA-CTD introduces a more modest (+) superhelicity. The observation of a superhelical spiral in the present structure and that of the Bacillus stearothermophilus ParC-CTD structure suggests unexpected similarities in substrate selectivity between gyrase and Topo IV enzymes. We propose a model wherein the right-handed ((+) solenoidal) wrapping of DNA around the E. coli GyrA-CTD enforces unidirectional (-) DNA supercoiling.

About this Structure

1ZI0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A superhelical spiral in the Escherichia coli DNA gyrase A C-terminal domain imparts unidirectional supercoiling bias., Ruthenburg AJ, Graybosch DM, Huetsch JC, Verdine GL, J Biol Chem. 2005 Jul 15;280(28):26177-84. Epub 2005 May 15. PMID:15897198

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