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rdf:type |
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lifeskim:mentions |
umls-concept:C0026649,
umls-concept:C0035495,
umls-concept:C0037083,
umls-concept:C0041249,
umls-concept:C0057683,
umls-concept:C1442792,
umls-concept:C1514562,
umls-concept:C1710082,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2603343
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pubmed:issue |
42
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pubmed:dateCreated |
2009-10-20
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pubmed:abstractText |
Previous crystallographic studies of the AppA BLUF domain indicated that Trp104 is capable of undertaking alternate conformations depending on the length of the BLUF domain. A BLUF domain containing a C-terminal deletion (AppA1-126) reveals that Trp104 is partially solvent exposed while a BLUF domain containing a slightly longer carboxyl terminal region (AppA17-133) shows that Trp104 is deeply buried. This observation has led to a model proposing that Trp104 moves from a deeply buried position in the dark state to a solvent-exposed position in the light excited state. In this study we investigated whether there is indeed movement of Trp104 upon light excitation using a combination of NMR and absorption spectroscopy, steady-state fluorescence, and acrylamide quenching of tryptophan fluorescence. Our results indicate that AppA17-133 and AppA1-126 contain Trp104 in distinct alternate conformations in solution and that light absorption by the flavin causes partial movement/uncovering of Trp104. However, we conclude that light exposure does not cause dramatic change of Trp104 from "Trp-in" to "Trp-out" conformations (or vice versa) upon light absorption. These results do not support a model of Trp104 movement as a key output signal.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-12230978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-1252418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-15570388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-15667215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-15793585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-15876364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-15924418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16002996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16107542,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16204305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16331957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16388580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16637622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16829579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-16949615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-17042486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-17117839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-18263659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-18435699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-18722438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-18771279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-5119250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-7037051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19746968-9857073
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
27
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9969-79
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:19746968-Bacterial Proteins,
pubmed-meshheading:19746968-Flavoproteins,
pubmed-meshheading:19746968-Magnetic Resonance Spectroscopy,
pubmed-meshheading:19746968-Models, Molecular,
pubmed-meshheading:19746968-Mutation,
pubmed-meshheading:19746968-Protein Structure, Tertiary,
pubmed-meshheading:19746968-Rhodobacter sphaeroides,
pubmed-meshheading:19746968-Signal Transduction,
pubmed-meshheading:19746968-Tryptophan
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pubmed:year |
2009
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pubmed:articleTitle |
Spectroscopic studies of the AppA BLUF domain from Rhodobacter sphaeroides: addressing movement of tryptophan 104 in the signaling state.
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pubmed:affiliation |
Departments of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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