1srx: Difference between revisions

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[[Image:1srx.gif|left|200px]]
{{Seed}}
[[Image:1srx.png|left|200px]]


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{{STRUCTURE_1srx|  PDB=1srx  |  SCENE=  }}  
{{STRUCTURE_1srx|  PDB=1srx  |  SCENE=  }}  


'''THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION'''
===THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION===




==Overview==
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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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{{ABSTRACT_PUBMED_1094461}}


==About this Structure==
==About this Structure==
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[[Category: Soderberg, B O.]]
[[Category: Soderberg, B O.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
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