1a69: Difference between revisions

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[[Category: transferase]]
[[Category: transferase]]


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Revision as of 15:40, 30 October 2007

File:1a69.gif


1a69, resolution 2.1Å

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PURINE NUCLEOSIDE PHOSPHORYLASE IN COMPLEX WITH FORMYCIN B AND SULPHATE (PHOSPHATE)

OverviewOverview

The ternary complex of purine nucleoside phosphorylase from E. coli with, formycin B and a sulphate or phosphate ion crystallized in the hexagonal, space group P6122 with unit cell dimensions a=123.11, c=241.22 A and three, monomers per asymmetric unit. The biologically active hexamer is formed, through 2-fold crystallographic symmetry, constituting a trimer of dimers., High-resolution X-ray diffraction data were collected using synchrotron, radiation (Daresbury, England). The crystal structure was determined by, molecular replacement and refined at 2.1 A resolution to an R-value of, 0.196.There is one active centre per monomer, composed of residues, belonging to two subunits of one dimer. The phosphate binding site is, strongly positively charged and consists of three arginine residues, ... [(full description)]

About this StructureAbout this Structure

1A69 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 and FMB as [ligands]. Active as [Purine-nucleoside phosphorylase], with EC number [2.4.2.1]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution., Koellner G, Luic M, Shugar D, Saenger W, Bzowska A, J Mol Biol. 1998 Jul 3;280(1):153-66. PMID:9653038

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OCA