1srx

<table><tr><td colspan='2'>[[1srx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_(strain_b) Escherichia coli (strain b)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SRX FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1srx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srx OCA], [https://pdbe.org/1srx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1srx RCSB], [https://www.ebi.ac.uk/pdbsum/1srx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1srx ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.

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== Publication Abstract from PubMed ==

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.

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution.,Holmgren A, Soderberg BO, Eklund H, Branden CI Proc Natl Acad Sci U S A. 1975 Jun;72(6):2305-9. PMID:1094461<ref>PMID:1094461</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Soderberg, B O]]

[[Category: Electron transport]]