2o8v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2o8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o8v, resolution 3.000&Aring;" /> '''PAPS reductase in a...)
Line 1: Line 1:
-
[[Image:2o8v.gif|left|200px]]<br /><applet load="2o8v" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2o8v.gif|left|200px]]<br /><applet load="2o8v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2o8v, resolution 3.000&Aring;" />
caption="2o8v, resolution 3.000&Aring;" />
'''PAPS reductase in a covalent complex with thioredoxin C35A'''<br />
'''PAPS reductase in a covalent complex with thioredoxin C35A'''<br />
==Overview==
==Overview==
-
The crystal structure of Escherichia coli, 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E., coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two, proteins are covalently linked via a mixed disulfide that forms during, nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the, PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate, in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting, an array of interprotein salt bridges between Trx and the strictly, conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The, structure also reveals a Trx-binding surface adjacent to the active site, cleft and regions of PAPS reductase associated with conformational change., Interaction at this site strategically positions Trx to bind the, S-sulfated C-terminus and addresses the mechanism for requisite structural, rearrangement of this domain. An apparent sulfite-binding pocket at the, protein-protein interface explicitly orients the S-sulfocysteine Sgamma, atom for nucleophilic attack in a subsequent step. Taken together, the, structure of PAPS reductase in complex with Trx highlights the large, structural rearrangement required to accomplish sulfonucleotide reduction, and suggests a role for Trx in catalysis beyond the paradigm of disulfide, reduction.
+
The crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E. coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting an array of interprotein salt bridges between Trx and the strictly conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The structure also reveals a Trx-binding surface adjacent to the active site cleft and regions of PAPS reductase associated with conformational change. Interaction at this site strategically positions Trx to bind the S-sulfated C-terminus and addresses the mechanism for requisite structural rearrangement of this domain. An apparent sulfite-binding pocket at the protein-protein interface explicitly orients the S-sulfocysteine Sgamma atom for nucleophilic attack in a subsequent step. Taken together, the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
==About this Structure==
==About this Structure==
-
2O8V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O8V OCA].
+
2O8V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Phosphoadenylyl-sulfate_reductase_(thioredoxin) Phosphoadenylyl-sulfate reductase (thioredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.8 1.8.4.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O8V OCA].
==Reference==
==Reference==
-
3'-Phosphoadenosine-5'-phosphosulfate Reductase in Complex with Thioredoxin: A Structural Snapshot in the Catalytic Cycle(,)., Chartron J, Shiau C, Stout CD, Carroll KS, Biochemistry. 2007 Apr 3;46(13):3942-3951. Epub 2007 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17352498 17352498]
+
3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle., Chartron J, Shiau C, Stout CD, Carroll KS, Biochemistry. 2007 Apr 3;46(13):3942-51. Epub 2007 Mar 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17352498 17352498]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Phosphoadenylyl-sulfate reductase (thioredoxin)]]
[[Category: Phosphoadenylyl-sulfate reductase (thioredoxin)]]
[[Category: Protein complex]]
[[Category: Protein complex]]
-
[[Category: Carroll, K.S.]]
+
[[Category: Carroll, K S.]]
[[Category: Chartron, J.]]
[[Category: Chartron, J.]]
[[Category: Shiau, C.]]
[[Category: Shiau, C.]]
-
[[Category: Stout, C.D.]]
+
[[Category: Stout, C D.]]
[[Category: disulfide crosslinked complex]]
[[Category: disulfide crosslinked complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:05:22 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:45 2008''

Revision as of 16:15, 21 February 2008


2o8v, resolution 3.000Å

Drag the structure with the mouse to rotate

PAPS reductase in a covalent complex with thioredoxin C35A

Overview

The crystal structure of Escherichia coli 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase in complex with E. coli thioredoxin 1 (Trx1) has been determined to 3.0 A resolution. The two proteins are covalently linked via a mixed disulfide that forms during nucleophilic attack of Trx's N-terminal cysteine on the Sgamma atom of the PAPS reductase S-sulfocysteine (E-Cys-Sgamma-SO3-), a central intermediate in the catalytic cycle. For the first time in a crystal structure, residues 235-244 in the PAPS reductase C-terminus are observed, depicting an array of interprotein salt bridges between Trx and the strictly conserved glutathione-like sequence, Glu238Cys239Gly240Leu241His242. The structure also reveals a Trx-binding surface adjacent to the active site cleft and regions of PAPS reductase associated with conformational change. Interaction at this site strategically positions Trx to bind the S-sulfated C-terminus and addresses the mechanism for requisite structural rearrangement of this domain. An apparent sulfite-binding pocket at the protein-protein interface explicitly orients the S-sulfocysteine Sgamma atom for nucleophilic attack in a subsequent step. Taken together, the structure of PAPS reductase in complex with Trx highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.

About this Structure

2O8V is a Protein complex structure of sequences from Escherichia coli. Active as Phosphoadenylyl-sulfate reductase (thioredoxin), with EC number 1.8.4.8 Full crystallographic information is available from OCA.

Reference

3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle., Chartron J, Shiau C, Stout CD, Carroll KS, Biochemistry. 2007 Apr 3;46(13):3942-51. Epub 2007 Mar 13. PMID:17352498

Page seeded by OCA on Thu Feb 21 18:15:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools