This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1srx
From Proteopedia
(New page: 200px<br /><applet load="1srx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1srx, resolution 2.8Å" /> '''THREE-DIMENSIONAL STR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1srx.gif|left|200px]]<br /><applet load="1srx" size=" | + | [[Image:1srx.gif|left|200px]]<br /><applet load="1srx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1srx, resolution 2.8Å" /> | caption="1srx, resolution 2.8Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN-S2 TO 2.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the electron transport protein | + | 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== | ==About this Structure== | ||
| - | 1SRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_b Escherichia coli b]. Full crystallographic information is available from [http:// | + | 1SRX is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli b]] | [[Category: Escherichia coli b]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Soderberg, B | + | [[Category: Soderberg, B O.]] |
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:36 2008'' |
Revision as of 13:04, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 15:04:36 2008
