1mu5
From Proteopedia
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|PDB= 1mu5 |SIZE=350|CAPTION= <scene name='initialview01'>1mu5</scene>, resolution 2.000Å | |PDB= 1mu5 |SIZE=350|CAPTION= <scene name='initialview01'>1mu5</scene>, resolution 2.000Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
- | |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] | + | |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= top6b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 Sulfolobus shibatae]) | |GENE= top6b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 Sulfolobus shibatae]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1mx0|1MX0]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu5 OCA], [http://www.ebi.ac.uk/pdbsum/1mu5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mu5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Berger, J M.]] | [[Category: Berger, J M.]] | ||
[[Category: Corbett, K D.]] | [[Category: Corbett, K D.]] | ||
- | [[Category: CA]] | ||
[[Category: ghkl atpase]] | [[Category: ghkl atpase]] | ||
[[Category: helix two-turns helix]] | [[Category: helix two-turns helix]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:21:09 2008'' |
Revision as of 19:21, 30 March 2008
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, resolution 2.000Å | |||||||
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Ligands: | |||||||
Gene: | top6b (Sulfolobus shibatae) | ||||||
Activity: | DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 | ||||||
Related: | 1MX0
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of topoisomerase subunit
Overview
Type IIA and type IIB topoisomerases each possess the ability to pass one DNA duplex through another in an ATP-dependent manner. The role of ATP in the strand passage reaction is poorly understood, particularly for the type IIB (topoisomerase VI) family. We have solved the structure of the ATP-binding subunit of topoisomerase VI (topoVI-B) in two states: an unliganded monomer and a nucleotide-bound dimer. We find that topoVI-B is highly structurally homologous to the entire 40-43 kDa ATPase region of type IIA topoisomerases and MutL proteins. Nucleotide binding to topoVI-B leads to dimerization of the protein and causes dramatic conformational changes within each protomer. Our data demonstrate that type IIA and type IIB topoisomerases have descended from a common ancestor and reveal how ATP turnover generates structural signals in the reactions of both type II topoisomerase families. When combined with the structure of the A subunit to create a picture of the intact topoisomerase VI holoenzyme, the ATP-driven motions of topoVI-B reveal a simple mechanism for strand passage by the type IIB topoisomerases.
About this Structure
1MU5 is a Single protein structure of sequence from Sulfolobus shibatae. Full crystallographic information is available from OCA.
Reference
Structure of the topoisomerase VI-B subunit: implications for type II topoisomerase mechanism and evolution., Corbett KD, Berger JM, EMBO J. 2003 Jan 2;22(1):151-63. PMID:12505993
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