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| {{STRUCTURE_1jed| PDB=1jed | SCENE= }} | | {{STRUCTURE_1jed| PDB=1jed | SCENE= }} |
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| '''Crystal Structure of ATP Sulfurylase in complex with ADP'''
| | ===Crystal Structure of ATP Sulfurylase in complex with ADP=== |
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| ==Overview==
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| The ubiquitous enzyme ATP sulfurylase (ATPS) catalyzes the primary step of intracellular sulfate activation, the formation of adenosine 5'-phosphosulfate (APS). It has been shown that the enzyme catalyzes the generation of APS from ATP and inorganic sulfate in vitro and in vivo, and that this reaction can be inhibited by a number of simple molecules. Here, we present the crystal structures of ATPS from the yeast Saccharomyces cerevisiae complexed with compounds that have inhibitory effects on the catalytic reaction of ATPS. Thiosulfate and ADP mimic the substrates sulfate and ATP in the active site, but are non-reactive and thus competitive inhibitors of the sulfurylase reaction. Chlorate is bound in a crevice between the active site and the intermediate domain III of the complex structure. It forms hydrogen bonds to residues of both domains and stabilizes a "closed" conformation, inhibiting the release of the reaction products APS and PPi. These new observations are evidence for the crucial role of the displacement mechanism for the catalysis by ATPS. | | The line below this paragraph, {{ABSTRACT_PUBMED_11700067}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11700067 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11700067}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Inhibitor complex]] | | [[Category: Inhibitor complex]] |
| [[Category: Rossmann-fold]] | | [[Category: Rossmann-fold]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:06:54 2008'' |