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| [[Image:1nqz.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1nqz.png|left|200px]] |
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| {{STRUCTURE_1nqz| PDB=1nqz | SCENE= }} | | {{STRUCTURE_1nqz| PDB=1nqz | SCENE= }} |
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| '''The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion'''
| | ===The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion=== |
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| ==Overview==
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| Gene Dr1184 from Deinococcus radiodurans codes for a Nudix enzyme (DR-CoAse) that hydrolyzes the pyrophosphate moiety of coenzyme A (CoA). Nudix enzymes with the same specificity have been found in yeast, humans, and mice. The three-dimensional structure of DR-CoAse, the first of a Nudix hydrolase with this specificity, reveals that this enzyme contains, in addition to the fold observed in other Nudix enzymes, insertions that are characteristic of a CoA-hydrolyzing Nudix subfamily. The structure of the complex of the enzyme with Mg(2+), its activating cation, reveals the position of the catalytic site. A helix, part of the N-terminal insertion, partially occludes the binding site and has to change its position to permit substrate binding. Comparison of the structure of DR-CoAse to those of other Nudix enzymes, together with the location in the structure of the sequence characteristic of CoAses, suggests a mode of binding of the substrate to the enzyme that is compatible with all available data.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12837785}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12837785 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12837785}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nudix]] | | [[Category: Nudix]] |
| [[Category: Pyrophosphatase]] | | [[Category: Pyrophosphatase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:52:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:39:25 2008'' |