pubmed-article:17766384 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0315191 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:17766384 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
pubmed-article:17766384 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:17766384 | pubmed:dateCreated | 2007-9-3 | lld:pubmed |
pubmed-article:17766384 | pubmed:abstractText | Among the transcription factors, the helix-turn-helix (HTH) GntR family comprised of FadR, HutC, MocR, YtrA, AraR, and PlmA subfamilies regulates the most varied biological processes. Generally, proteins belonging to this family contain an N-terminal DNA-binding domain and a C-terminal effector-binding/oligomerization domain. The members of the YtrA subfamily are much shorter than other members of this family, with chain lengths of 120-130 residues with about 50 residues located in the C-terminal domain. Because of this length, the mode of dimerization and the ability to bind effectors by the C-terminal domain are puzzling. Here, we first report the structure of the transcription factor CGL2947 from Corynebacterium glutamicum, which belongs to the YtrA family. The monomer is composed of a DNA-binding domain containing a winged HTH motif in the N terminus and two helices (alpha4 and alpha5) with a fishhook-shaped arrangement in the C terminus. Helices alpha4 and alpha5 of two monomers intertwine together to form a novel homodimer assembly. The effector-accommodating pocket with 2-methyl-2,4-pentanediol (MPD) docked was located, and it was suggested to represent a novel mode of effector binding. The structures in two crystal forms (MPD-free and -bound in the proposed effector-binding pocket) were solved. The structural variations have implications regarding how the effector-induced conformational change modulates DNA affinity for YtrA family members. | lld:pubmed |
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pubmed-article:17766384 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17766384 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:language | eng | lld:pubmed |
pubmed-article:17766384 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17766384 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17766384 | pubmed:month | Sep | lld:pubmed |
pubmed-article:17766384 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:17766384 | pubmed:author | pubmed-author:KenY HYH | lld:pubmed |
pubmed-article:17766384 | pubmed:author | pubmed-author:TanakaIsaoI | lld:pubmed |
pubmed-article:17766384 | pubmed:author | pubmed-author:ItouHiroshiH | lld:pubmed |
pubmed-article:17766384 | pubmed:author | pubmed-author:ZhouYongY | lld:pubmed |
pubmed-article:17766384 | pubmed:author | pubmed-author:GaoYong-GuiYG | lld:pubmed |
pubmed-article:17766384 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17766384 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:17766384 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17766384 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17766384 | pubmed:pagination | 1878-86 | lld:pubmed |
pubmed-article:17766384 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:17766384 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17766384 | pubmed:articleTitle | The structures of transcription factor CGL2947 from Corynebacterium glutamicum in two crystal forms: a novel homodimer assembling and the implication for effector-binding mode. | lld:pubmed |
pubmed-article:17766384 | pubmed:affiliation | Faculty of Advanced Life Sciences, Hokkaido University, Sapporo 060-0810, Japan. | lld:pubmed |
pubmed-article:17766384 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17766384 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17766384 | lld:pubmed |