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2o8v
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= cysH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= cysH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1sur|1SUR]], [[2trx|2TRX]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o8v OCA], [http://www.ebi.ac.uk/pdbsum/2o8v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2o8v RCSB]</span> | ||
}} | }} | ||
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[[Category: disulfide crosslinked complex]] | [[Category: disulfide crosslinked complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:14:21 2008'' |
Revision as of 01:14, 31 March 2008
| |||||||
| , resolution 3.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | cysH (Escherichia coli), trxA (Escherichia coli) | ||||||
| Activity: | Phosphoadenylyl-sulfate reductase (thioredoxin), with EC number 1.8.4.8 | ||||||
| Related: | 1SUR, 2TRX
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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