1jnr
From Proteopedia
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|PDB= 1jnr |SIZE=350|CAPTION= <scene name='initialview01'>1jnr</scene>, resolution 1.60Å | |PDB= 1jnr |SIZE=350|CAPTION= <scene name='initialview01'>1jnr</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase Adenylyl-sulfate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.99.2 1.8.99.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylyl-sulfate_reductase Adenylyl-sulfate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.99.2 1.8.99.2] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jnr OCA], [http://www.ebi.ac.uk/pdbsum/1jnr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jnr RCSB]</span> | ||
}} | }} | ||
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[[Category: Schiffer, A.]] | [[Category: Schiffer, A.]] | ||
[[Category: Stetter, K O.]] | [[Category: Stetter, K O.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SF4]] | ||
[[Category: sulfur metabolism/ adenylylsulfate reductase/ iron-sulfur flavoprotein/ crystal structure/catalysis]] | [[Category: sulfur metabolism/ adenylylsulfate reductase/ iron-sulfur flavoprotein/ crystal structure/catalysis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:36:17 2008'' |
Revision as of 18:36, 30 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Adenylyl-sulfate reductase, with EC number 1.8.99.2 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6 resolution
Overview
The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5'-phosphosulfate, APS) reductase catalyzes reversibly the reduction of APS to sulfite and AMP. The structures of APS reductase from the hyperthermophilic Archaeoglobus fulgidus in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6- and 2.5- resolution, respectively. The FAD-sulfite adduct was detected after soaking the crystals with APS. This finding and the architecture of the active site strongly suggest that catalysis involves a nucleophilic attack of the N5 atom of reduced FAD on the sulfur atom of APS. In view of the high degree of similarity between APS reductase and fumarate reductase especially with regard to the FAD-binding alpha-subunit, it is proposed that both subunits originate from a common ancestor resembling archaeal APS reductase. The two electrons required for APS reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The exceptionally large difference in reduction potential of these clusters (-60 and -500 mV) can be explained by interactions of the clusters with the protein matrix.
About this Structure
1JNR is a Protein complex structure of sequences from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution., Fritz G, Roth A, Schiffer A, Buchert T, Bourenkov G, Bartunik HD, Huber H, Stetter KO, Kroneck PM, Ermler U, Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1836-41. Epub 2002 Feb 12. PMID:11842205
Page seeded by OCA on Sun Mar 30 21:36:17 2008
Categories: Adenylyl-sulfate reductase | Archaeoglobus fulgidus | Protein complex | Bartunik, H D. | Bourenkov, G. | Buechert, T. | Ermler, U. | Fritz, G. | Huber, H. | Kroneck, P M.H. | Roth, A. | Schiffer, A. | Stetter, K O. | Sulfur metabolism/ adenylylsulfate reductase/ iron-sulfur flavoprotein/ crystal structure/catalysis
