1odi
|
PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS
OverviewOverview
The purine nucleoside phosphorylase from Thermus thermophilus crystallized, in space group P4(3)2(1)2 with the unit cell dimensions a = 131.9 A and c, = 169.9 A and one biologically active hexamer in the asymmetric unit. The, structure was solved by the molecular replacement method and refined at a, 1.9A resolution to an r(free) value of 20.8%. The crystals of the binary, complex with sulfate ion and ternary complexes with sulfate and adenosine, or guanosine were also prepared and their crystal structures were refined, at 2.1A, 2.4A and 2.4A, respectively. The overall structure of the, T.thermophilus enzyme is similar to the structures of hexameric enzymes, from Escherichia coli and Sulfolobus solfataricus, but significant, differences are observed in the purine base recognition site. A ... [(full description)]
About this StructureAbout this Structure
1ODI is a [Single protein] structure of sequence from [Thermus thermophilus] with SO4 and ADN as [ligands]. Active as [S-methyl-5-thioadenosine phosphorylase], with EC number [2.4.2.28]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of purine nucleoside phosphorylase from Thermus thermophilus., Tahirov TH, Inagaki E, Ohshima N, Kitao T, Kuroishi C, Ukita Y, Takio K, Kobayashi M, Kuramitsu S, Yokoyama S, Miyano M, J Mol Biol. 2004 Apr 9;337(5):1149-60. PMID:15046984
Page seeded by OCA on Tue Oct 30 15:50:37 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- S-methyl-5-thioadenosine phosphorylase
- Single protein
- Thermus thermophilus
- Inagaki, E.
- Miyano, M.
- RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.
- Tahirov, T.H.
- ADN
- SO4
- Adenosine
- Alpha-beta protein
- Nucleoside phosphorylase
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomics