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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1975-9-9
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-14245400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4118873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4145325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4352363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4361672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4365379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4367210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4368490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4374553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4382243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4521211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4552684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4587639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4616096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4737475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4809626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4841001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4843141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4883076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4924205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-4945270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-5442277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-5451100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-5685102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-5760491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1094461-803502
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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 |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
72
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2305-9
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pubmed:dateRevised |
2010-9-3
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pubmed:meshHeading |
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pubmed:year |
1975
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pubmed:articleTitle |
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.
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pubmed:publicationType |
Journal Article
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