1srx: Difference between revisions
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'''THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1srx |SIZE=350|CAPTION= <scene name='initialview01'>1srx</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SRX is a [ | 1SRX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_b Escherichia coli b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRX OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1094461 1094461] | ||
[[Category: Escherichia coli b]] | [[Category: Escherichia coli b]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:52 2008'' | ||
Revision as of 12:08, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1SRX is a Single protein structure of sequence from Escherichia coli b. Full crystallographic information is available from OCA.
Reference
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
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