1nqz: Difference between revisions
New page: left|200px<br /><applet load="1nqz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nqz, resolution 1.7Å" /> '''The structure of a Co... |
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[[Image:1nqz.jpg|left|200px]]<br /><applet load="1nqz" size=" | [[Image:1nqz.jpg|left|200px]]<br /><applet load="1nqz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nqz, resolution 1.7Å" /> | caption="1nqz, resolution 1.7Å" /> | ||
'''The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion'''<br /> | '''The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion'''<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== | ||
1NQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 1NQZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1NQZ 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: MG]] | [[Category: MG]] | ||
[[Category: coa]] | [[Category: coa]] | ||
[[Category: d | [[Category: d radiodurans]] | ||
[[Category: mutt]] | [[Category: mutt]] | ||
[[Category: nudix]] | [[Category: nudix]] | ||
[[Category: pyrophosphatase]] | [[Category: pyrophosphatase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:13 2008'' | ||
Revision as of 15:09, 21 February 2008
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The structure of a CoA pyrophosphatase from D. Radiodurans complexed with a magnesium ion
OverviewOverview
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 StructureAbout this Structure
1NQZ is a Single protein structure of sequence from Deinococcus radiodurans with as ligand. Active as Nucleotide diphosphatase, with EC number 3.6.1.9 Full crystallographic information is available from OCA.
ReferenceReference
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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