1h4m: Difference between revisions

Revision as of 06:36, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1h4m.png

Template:STRUCTURE 1h4m

SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATESULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE

Template:ABSTRACT PUBMED 11592406

About this StructureAbout this Structure

1H4M 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

Page seeded by OCA on Tue Jul 1 06:36:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1h4m.gif|left|200px]]
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 {{STRUCTURE_1h4m|  PDB=1h4m  |  SCENE=  }}
-'''SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE'''
+===SULFURTRANSFERASE FROM AZOTOBACTER VINELANDII IN COMPLEX WITH PHOSPHATE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11592406}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11592406 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11592406}}
 ==About this Structure==
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 [[Category: Sulfurtransferase]]
 [[Category: Thiosulfate:cyanide]]
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