1nqy
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= Dr1184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans]) | |GENE= Dr1184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1299 Deinococcus radiodurans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1nqz|1NQZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nqy OCA], [http://www.ebi.ac.uk/pdbsum/1nqy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nqy RCSB]</span> | ||
}} | }} | ||
| Line 34: | Line 37: | ||
[[Category: pyrophosphatase]] | [[Category: pyrophosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:34:19 2008'' |
Revision as of 19:34, 30 March 2008
| |||||||
| , resolution 2.09Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | Dr1184 (Deinococcus radiodurans) | ||||||
| Activity: | Nucleotide diphosphatase, with EC number 3.6.1.9 | ||||||
| Related: | 1NQZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 22:34:19 2008
