1srx: Difference between revisions
New page: left|200px<br /><applet load="1srx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1srx, resolution 2.8Å" /> '''THREE-DIMENSIONAL STR... |
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[[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== | ||
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[[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
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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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