1h4m: Difference between revisions
New page: left|200px<br /><applet load="1h4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4m, resolution 2.1Å" /> '''SULFURTRANSFERASE FRO... |
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[[Image:1h4m.gif|left|200px]]<br /><applet load="1h4m" size=" | [[Image:1h4m.gif|left|200px]]<br /><applet load="1h4m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1h4m, resolution 2.1Å" /> | caption="1h4m, resolution 2.1Å" /> | ||
'''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE'''<br /> | '''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE'''<br /> | ||
==Overview== | ==Overview== | ||
Active site reactivity and specificity of RhdA, a thiosulfate:cyanide | 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 Structure== | ==About this Structure== | ||
1H4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1H4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4M OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thiosulfate:cyanide]] | [[Category: thiosulfate:cyanide]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:20 2008'' | ||
Revision as of 13:57, 21 February 2008
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SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE
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
1H4M is a Single protein structure of sequence from Azotobacter vinelandii with as ligand. Active as Thiosulfate sulfurtransferase, with EC number 2.8.1.1 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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