1nqy
From Proteopedia
(New page: 200px<br /><applet load="1nqy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nqy, resolution 2.09Å" /> '''The structure of a C...) |
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| - | [[Image:1nqy.jpg|left|200px]]<br /><applet load="1nqy" size=" | + | [[Image:1nqy.jpg|left|200px]]<br /><applet load="1nqy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nqy, resolution 2.09Å" /> | caption="1nqy, resolution 2.09Å" /> | ||
'''The structure of a CoA pyrophosphatase from D. Radiodurans'''<br /> | '''The structure of a CoA pyrophosphatase from D. Radiodurans'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Gene Dr1184 from Deinococcus radiodurans codes for a Nudix enzyme | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Active as [http://en.wikipedia.org/wiki/Nucleotide_diphosphatase Nucleotide diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.9 3.6.1.9] Full crystallographic information is available from [http:// | + | 1NQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Active as [http://en.wikipedia.org/wiki/Nucleotide_diphosphatase Nucleotide diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.9 3.6.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nucleotide diphosphatase]] | [[Category: Nucleotide diphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Bessman, M | + | [[Category: Bessman, M J.]] |
| - | [[Category: Bianchet, M | + | [[Category: Bianchet, M A.]] |
| - | [[Category: Gabelli, S | + | [[Category: Gabelli, S B.]] |
| - | [[Category: Kang, L | + | [[Category: Kang, L W.]] |
| - | [[Category: Xu, W | + | [[Category: Xu, W L.]] |
[[Category: coa]] | [[Category: coa]] | ||
[[Category: dr1184]] | [[Category: dr1184]] | ||
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[[Category: pyrophosphatase]] | [[Category: pyrophosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:03 2008'' |
Revision as of 12:09, 21 February 2008
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The structure of a CoA pyrophosphatase from D. Radiodurans
Overview
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.
About this Structure
1NQY is a Single protein structure of sequence from Deinococcus radiodurans. Active as Nucleotide diphosphatase, with EC number 3.6.1.9 Full crystallographic information is available from OCA.
Reference
Structure of a coenzyme A pyrophosphatase from Deinococcus radiodurans: a member of the Nudix family., Kang LW, Gabelli SB, Bianchet MA, Xu WL, Bessman MJ, Amzel LM, J Bacteriol. 2003 Jul;185(14):4110-8. PMID:12837785
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