1w2y: Difference between revisions
No edit summary |
No edit summary |
||
| Line 31: | Line 31: | ||
[[Category: pathogen]] | [[Category: pathogen]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:23:17 2007'' | ||
Revision as of 17:18, 30 October 2007
|
THE CRYSTAL STRUCTURE OF A COMPLEX OF CAMPYLOBACTER JEJUNI DUTPASE WITH SUBSTRATE ANALOGUE DUPNHP
OverviewOverview
The crystal structure of the dUTPase from the important gastric pathogen, Campylobacter jejuni has been solved at 1.65 A spacing. This essential, bacterial enzyme is the second representative of the new family of dimeric, dUTPases to be structurally characterised. Members of this family have a, novel all-alpha fold and are unrelated to the all-beta dUTPases of the, majority of organisms including eukaryotes such as humans, bacteria such, as Escherichia coli, archaea like Methanococcus jannaschii and animal, viruses. Therefore, dimeric dUTPases can be considered as candidate drug, targets. The X-ray structure of the C.jejuni dUTPase in complex with the, non-hydrolysable substrate analogue dUpNHp allows us to define the, positions of three catalytically significant phosphate-binding ... [(full description)]
About this StructureAbout this Structure
1W2Y is a [Single protein] structure of sequence from [Campylobacter jejuni] with MG and DUN as [ligands]. Active as [dUTP diphosphatase], with EC number [3.6.1.23]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases., Moroz OV, Harkiolaki M, Galperin MY, Vagin AA, Gonzalez-Pacanowska D, Wilson KS, J Mol Biol. 2004 Oct 1;342(5):1583-97. PMID:15364583
Page seeded by OCA on Tue Oct 30 16:23:17 2007