1h4k: Difference between revisions
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[[Image:1h4k.gif|left|200px]] | [[Image:1h4k.gif|left|200px]] | ||
'''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH HYPOPHOSPHITE''' | {{Structure | ||
|PDB= 1h4k |SIZE=350|CAPTION= <scene name='initialview01'>1h4k</scene>, resolution 2.05Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PO2:HYPOPHOSPHITE'>PO2</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Thiosulfate_sulfurtransferase Thiosulfate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.1 2.8.1.1] | |||
|GENE= RHDA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii]) | |||
}} | |||
'''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH HYPOPHOSPHITE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1H4K is a [ | 1H4K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4K OCA]. | ||
==Reference== | ==Reference== | ||
A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese., Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S, Biol Chem. 2001 Aug;382(8):1245-52. PMID:[http:// | A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese., Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S, Biol Chem. 2001 Aug;382(8):1245-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11592406 11592406] | ||
[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thiosulfate:cyanide]] | [[Category: thiosulfate:cyanide]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:32:06 2008'' | ||
Revision as of 12:32, 20 March 2008
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | RHDA (Azotobacter vinelandii) | ||||||
| Activity: | Thiosulfate sulfurtransferase, with EC number 2.8.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH HYPOPHOSPHITE
OverviewOverview
Active site reactivity and specificity of RhdA, a thiosulfate:cyanide sulfurtransferase (rhodanese) from Azotobacter vinelandii, have been investigated through ligand binding, site-directed mutagenesis, and X-ray crystallographic techniques, in a combined approach. In native RhdA the active site Cys230 is found persulfurated; fluorescence and sulfurtransferase activity measurements show that phosphate anions interact with Cys230 persulfide sulfur atom and modulate activity. Crystallographic analyses confirm that phosphate and hypophosphite anions react with native RhdA, removing the persulfide sulfur atom from the active site pocket. Considering that RhdA and the catalytic subunit of Cdc25 phosphatases share a common three-dimensional fold as well as active site Cys (catalytic) and Arg residues, two RhdA mutants carrying a single amino acid insertion at the active site loop were designed and their phosphatase activity tested. The crystallographic and functional results reported here show that specific sulfurtransferase or phosphatase activities are strictly related to precise tailoring of the catalytic loop structure in RhdA and Cdc25 phosphatase, respectively.
About this StructureAbout this Structure
1H4K is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.
ReferenceReference
A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese., Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S, Biol Chem. 2001 Aug;382(8):1245-52. PMID:11592406
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