1a69: Difference between revisions

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[[Image:1a69.gif|left|200px]]
[[Image:1a69.gif|left|200px]]


{{Structure
<!--
|PDB= 1a69 |SIZE=350|CAPTION= <scene name='initialview01'>1a69</scene>, resolution 2.1&Aring;
The line below this paragraph, containing "STRUCTURE_1a69", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AVE:Binding+Site+Of+Formycin+B+And+Phosphate'>AVE</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=FMB:FORMYCIN+B'>FMB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1a69| PDB=1a69  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a69 OCA], [http://www.ebi.ac.uk/pdbsum/1a69 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a69 RCSB]</span>
}}


'''PURINE NUCLEOSIDE PHOSPHORYLASE IN COMPLEX WITH FORMYCIN B AND SULPHATE (PHOSPHATE)'''
'''PURINE NUCLEOSIDE PHOSPHORYLASE IN COMPLEX WITH FORMYCIN B AND SULPHATE (PHOSPHATE)'''
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[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
[[Category: Shugar, D.]]
[[Category: Shugar, D.]]
[[Category: glycosyltransferase]]
[[Category: Glycosyltransferase]]
[[Category: purine nucleoside phosphorylase]]
[[Category: Purine nucleoside phosphorylase]]
[[Category: transferase]]
[[Category: Transferase]]
 
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Revision as of 09:52, 2 May 2008

File:1a69.gif

Template:STRUCTURE 1a69

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 (Arg24, Arg87 and Arg43 from a neighbouring subunit), Ser90 and Gly20. It is occupied by a sulphate or phosphate anion, each oxygen atom of which accepts at least two hydrogen bonds or salt-bridges. The sulphate or phosphate anion is also in direct contact with the ribose moiety of formycin B. The ribose binding site is composed of Ser90, Met180, Glu181 and His4, the latter belonging to the neighbouring subunit. The base binding site is exposed to solvent, and the base is unspecifically bound through a chain of water molecules and aromatic-aromatic interactions. In all monomers the nucleosides are in the high syn conformation about the glycosidic bonds with chi in the range 100 to 130 degrees. The architecture of the active centre is in line with the known broad specificity and the kinetic properties of E. coli PNP.

About this StructureAbout this Structure

1A69 is a Single protein structure of sequence from Escherichia coli. 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 Page seeded by OCA on Fri May 2 09:52:28 2008

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