| pubmed-article:1094461 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1094461 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:1094461 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1094461 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:1094461 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:1094461 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1094461 | pubmed:dateCreated | 1975-9-9 | lld:pubmed |
| pubmed-article:1094461 | pubmed:abstractText | The three-dimensional structure of the electron transport protein thioredoxin-S2 from E. coli has been determined from a 2.8 A resolution electron density map. The molecule is built up of a central core of three parallel and two antiparallel strands of pleated sheet surrounded by four helices. Thr residues involved in the active center 14-membered disulfide ring of thioredoxin form a protrusion between one of the helices and the middle strand of the pleated sheet. This region of the molecule, comprising two parallel strands joined by the protrusion and a helix, is structurally very similar to corresponding functionally important regions in the nucleotide-binding domains of flavodoxin and the dehydrogenases. The molecule has about 75% of the residues in well-defined secondary structures. The structure indicates that the carboxy-terminal third of the molecule forms an independent folding unit consisting of two strands of antiparallel pleated sheet and a terminal alpha-helix. This agress with the noncovalent reconstitution experiments from thioredoxin peptide fragments. Thioredoxin is an example of a protein with the active center located on a protrusion rather than in a cleft, thus demonstrating the existence of male proteins. | lld:pubmed |
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| pubmed-article:1094461 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1094461 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1094461 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1094461 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1094461 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1094461 | pubmed:author | pubmed-author:HolmgrenAA | lld:pubmed |
| pubmed-article:1094461 | pubmed:author | pubmed-author:BrändénC ICI | lld:pubmed |
| pubmed-article:1094461 | pubmed:author | pubmed-author:EklundHH | lld:pubmed |
| pubmed-article:1094461 | pubmed:author | pubmed-author:SöderbergB... | lld:pubmed |
| pubmed-article:1094461 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1094461 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:1094461 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1094461 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1094461 | pubmed:pagination | 2305-9 | lld:pubmed |
| pubmed-article:1094461 | pubmed:dateRevised | 2010-9-3 | lld:pubmed |
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| pubmed-article:1094461 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:1094461 | pubmed:articleTitle | Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution. | lld:pubmed |
| pubmed-article:1094461 | pubmed:publicationType | Journal Article | lld:pubmed |
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