| pubmed-article:11914481 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11914481 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11914481 | lifeskim:mentions | umls-concept:C0221205 | lld:lifeskim |
| pubmed-article:11914481 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11914481 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:11914481 | lifeskim:mentions | umls-concept:C0054433 | lld:lifeskim |
| pubmed-article:11914481 | pubmed:issue | Pt 4 | lld:pubmed |
| pubmed-article:11914481 | pubmed:dateCreated | 2002-3-26 | lld:pubmed |
| pubmed-article:11914481 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:abstractText | A structural study is described of the photoactive yellow protein (PYP) reconstituted with the chromophore derivative 3,4-dihydroxycinnamic acid. The crystal structure of PYP reconstituted with this chromophore at 1.16 A resolution is reported in space group P6(5). This is the first high-resolution structure of a photoreceptor containing a modified chromophore. The introduction of an extra hydroxyl group in the native chromophore (i.e. p-coumaric acid) appears to perturb the structure of the hybrid yellow protein only slightly. The chromophore is bound by the protein in two different conformations, separated by a rotation of 180 degrees of the catechol ring. In combination with available spectroscopic data, it is concluded that the caffeic acid chromophore binds to the protein in a strained conformation, which leads to a faster ejection from the chromophore-binding pocket upon pB formation. | lld:pubmed |
| pubmed-article:11914481 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11914481 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11914481 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914481 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11914481 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11914481 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:11914481 | pubmed:author | pubmed-author:HellingwerfKl... | lld:pubmed |
| pubmed-article:11914481 | pubmed:author | pubmed-author:CrielaardWimW | lld:pubmed |
| pubmed-article:11914481 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:11914481 | pubmed:author | pubmed-author:Joshua-TorLee... | lld:pubmed |
| pubmed-article:11914481 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11914481 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:11914481 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11914481 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11914481 | pubmed:pagination | 585-90 | lld:pubmed |
| pubmed-article:11914481 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:11914481 | pubmed:meshHeading | pubmed-meshheading:11914481... | lld:pubmed |
| pubmed-article:11914481 | pubmed:meshHeading | pubmed-meshheading:11914481... | lld:pubmed |
| pubmed-article:11914481 | pubmed:meshHeading | pubmed-meshheading:11914481... | lld:pubmed |
| pubmed-article:11914481 | pubmed:meshHeading | pubmed-meshheading:11914481... | lld:pubmed |
| pubmed-article:11914481 | pubmed:meshHeading | pubmed-meshheading:11914481... | lld:pubmed |
| pubmed-article:11914481 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11914481 | pubmed:articleTitle | Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution. | lld:pubmed |
| pubmed-article:11914481 | pubmed:affiliation | W. M. Keck Structural Biology, Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA. | lld:pubmed |
| pubmed-article:11914481 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11914481 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11914481 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
