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| - | '''Crystal structure of the C-terminal domain of DNA topoisomerase IV'''
| + | ===Crystal structure of the C-terminal domain of DNA topoisomerase IV=== |
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| - | ==Overview==
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| - | Bacteria possess two closely related yet functionally distinct essential type IIA topoisomerases (Topos). DNA gyrase supports replication and transcription with its unique supercoiling activity, whereas Topo IV preferentially relaxes (+) supercoils and is a decatenating enzyme required for chromosome segregation. Here we report the crystal structure of the C-terminal domain of Topo IV ParC subunit (ParC-CTD) from Bacillus stearothermophilus and provide a structure-based explanation for how Topo IV and DNA gyrase execute distinct activities. Although the topological connectivity of ParC-CTD is similar to the recently determined CTD structure of DNA gyrase GyrA subunit (GyrA-CTD), ParC-CTD surprisingly folds as a previously unseen broken form of a six-bladed beta-propeller. Propeller breakage is due to the absence of a DNA gyrase-specific GyrA box motif, resulting in the reduction of curvature of the proposed DNA binding region, which explains why ParC-CTD is less efficient than GyrA-CTD in mediating DNA bending, a difference that leads to divergent activities of the two homologous enzymes. Moreover, we found that the topology of the propeller blades observed in ParC-CTD and GyrA-CTD can be achieved from a concerted beta-hairpin invasion-induced fold change event of a canonical six-bladed beta-propeller; hence, we proposed to name this new fold as "hairpin-invaded beta-propeller" to highlight the high degree of similarity and a potential evolutionary linkage between them. The possible role of ParC-CTD as a geometry facilitator during various catalytic events and the evolutionary relationships between prokaryotic type IIA Topos have also been discussed according to these new structural insights.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15466871}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15466871 is the PubMed ID number. |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hairpin-invaded beta-propeller]] | | [[Category: Hairpin-invaded beta-propeller]] |
| | [[Category: Six-bladed beta-propeller]] | | [[Category: Six-bladed beta-propeller]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:58:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:14:55 2008'' |
Revision as of 13:15, 28 July 2008
Template:STRUCTURE 1wp5
Crystal structure of the C-terminal domain of DNA topoisomerase IV
Template:ABSTRACT PUBMED 15466871
About this Structure
Full crystallographic information is available from OCA.
Reference
Structure of the topoisomerase IV C-terminal domain: a broken beta-propeller implies a role as geometry facilitator in catalysis., Hsieh TJ, Farh L, Huang WM, Chan NL, J Biol Chem. 2004 Dec 31;279(53):55587-93. Epub 2004 Oct 4. PMID:15466871
Page seeded by OCA on Mon Jul 28 16:14:55 2008
