1vfn
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1vfn.gif|left|200px]]<br /><applet load="1vfn" size=" | + | [[Image:1vfn.gif|left|200px]]<br /><applet load="1vfn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vfn, resolution 2.15Å" /> | caption="1vfn, resolution 2.15Å" /> | ||
'''PURINE NUCLEOSIDE PHOSPHORYLASE'''<br /> | '''PURINE NUCLEOSIDE PHOSPHORYLASE'''<br /> | ||
Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
- | 1VFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, ZN and HPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] Known structural/functional Sites: <scene name='pdbsite=BAS:Base Binding Site'>BAS</scene> and <scene name='pdbsite=PRE:Phosphate Binding Site'>PRE</scene>. Full crystallographic information is available from [http:// | + | 1VFN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=HPA:'>HPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] Known structural/functional Sites: <scene name='pdbsite=BAS:Base+Binding+Site'>BAS</scene> and <scene name='pdbsite=PRE:Phosphate+Binding+Site'>PRE</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VFN OCA]. |
==Reference== | ==Reference== | ||
Line 25: | Line 25: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:16:58 2008'' |
Revision as of 08:16, 3 February 2008
|
PURINE NUCLEOSIDE PHOSPHORYLASE
Overview
Trimeric calf spleen purine nucleoside phosphorylase has been complexed, with hypoxanthine via phosphorolysis of inosine in the presence of, phosphate. The resulting, "Michaelis" complex (three hypoxanthine, molecules per trimer), presumed to be formed under these conditions, crystallized in the cubic space group P2(1)3, with unit cell dimension a =, 94.11 A and one monomer in the asymmetric crystal unit; the biologically, active trimer is located on the crystallographic 3-fold axis., High-resolution X-ray diffraction data were collected using synchrotron, radiation (EMBL outstation, Hamburg, c/o DESY). The crystal structure has, been determined by molecular replacement and refined at 2.15 A resolution, to an R-value of 0.18. In the hypoxanthine binding site, a cis-peptide, bond between Asn243 and Lys244 is observed. Side-chains of GIu201 and, Asn243, as well as one integral water molecule located in the base binding, site, form hydrogen bonds with the hypoxanthine N-1 H, N-7 H and O-6. A, second water molecule links the base positions N-3 and N-9 with an, adjacent pocket, which presumably is the phosphate-binding site. This, pocket is filled completely by a cluster of six water molecules. Hence all, possible donor/acceptor-positions of hypoxanthine are saturated by, hydrogen-bonding to protein side-chains or integral water molecules., Purine nucleoside phosphorylase isolated form human tissues is a primary, target for chemotherapeutic intervention, and the more stable calf enzyme, has similar physico-chemical and kinetic properties, as well as response, to inhibitors. Hence the high-resolution structure presented here may, serve for design of inhibitors with potential pharmacological, applications.
About this Structure
1VFN is a Single protein structure of sequence from Bos taurus with , and as ligands. Active as Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution., Koellner G, Luic M, Shugar D, Saenger W, Bzowska A, J Mol Biol. 1997 Jan 17;265(2):202-16. PMID:9020983
Page seeded by OCA on Sun Feb 3 10:16:58 2008