1nqy: Difference between revisions

Revision as of 15:09, 21 February 2008

The structure of a CoA pyrophosphatase from D. Radiodurans

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

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.

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

Page seeded by OCA on Thu Feb 21 14:09:03 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nqy.jpg|left|200px]]<br /><applet load="1nqy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nqy.jpg|left|200px]]<br /><applet load="1nqy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nqy, resolution 2.09&Aring;" />
 '''The structure of a CoA pyrophosphatase from D. Radiodurans'''<br />
 ==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.
+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==
-NQY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NQY OCA].
+NQY 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==
@@ Line 14: / Line 14: @@
 [[Category: Nucleotide diphosphatase]]
 [[Category: Single protein]]
-[[Category: Amzel, L.M.]]
+[[Category: Amzel, L M.]]
-[[Category: Bessman, M.J.]]
+[[Category: Bessman, M J.]]
-[[Category: Bianchet, M.A.]]
+[[Category: Bianchet, M A.]]
-[[Category: Gabelli, S.B.]]
+[[Category: Gabelli, S B.]]
-[[Category: Kang, L.W.]]
+[[Category: Kang, L W.]]
-[[Category: Xu, W.L.]]
+[[Category: Xu, W L.]]
 [[Category: coa]]
 [[Category: dr1184]]
@@ Line 25: / Line 25: @@
 [[Category: pyrophosphatase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:36:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:03 2008''