| pubmed-article:21350762 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:21350762 | lifeskim:mentions | umls-concept:C0058597 | lld:lifeskim |
| pubmed-article:21350762 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:21350762 | pubmed:dateCreated | 2011-5-19 | lld:pubmed |
| pubmed-article:21350762 | pubmed:abstractText | Reverse gyrase introduces positive supercoils into DNA in an ATP-dependent process. It has a modular structure comprising a helicase-like and a topoisomerase domain. The helicase-like domain consists of two RecA-like subdomains and thus structurally resembles members of the helicase superfamily 2. It is a nucleotide-dependent switch that alters between an ATP state with a slight preference for dsDNA, and an ADP state with a high preference for ssDNA. Inter-domain communication between the helicase-like and the topoisomerase domain is central for their functional cooperation in reverse gyrase. The latch, an insertion into the helicase-like domain, has been suggested as an important element in coordinating their activities. Here, we have dissected the nucleotide cycle of the reverse gyrase helicase-like domain in the absence and presence of different DNA substrates. With this comprehensive thermodynamic characterization of the nucleotide cycle of the helicase-like domain, in combination with single molecule FRET data on the conformation of the helicase-like domain at all stages of the catalytic cycle, a picture emerges as to how the helicase-like domain may guide ATP-dependent positive supercoiling by reverse gyrase. | lld:pubmed |
| pubmed-article:21350762 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21350762 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21350762 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21350762 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:21350762 | pubmed:issn | 1463-9084 | lld:pubmed |
| pubmed-article:21350762 | pubmed:author | pubmed-author:KlostermeierD... | lld:pubmed |
| pubmed-article:21350762 | pubmed:author | pubmed-author:del Toro... | lld:pubmed |
| pubmed-article:21350762 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21350762 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:21350762 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:21350762 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21350762 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21350762 | pubmed:pagination | 10009-19 | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:meshHeading | pubmed-meshheading:21350762... | lld:pubmed |
| pubmed-article:21350762 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21350762 | pubmed:articleTitle | Nucleotide-driven conformational changes in the reverse gyrase helicase-like domain couple the nucleotide cycle to DNA processing. | lld:pubmed |
| pubmed-article:21350762 | pubmed:affiliation | University of Basel, Biozentrum, Dept. of Biophysical Chemistry, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. | lld:pubmed |
| pubmed-article:21350762 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21350762 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21350762 | lld:entrezgene |
