1onc
From Proteopedia
(New page: 200px<br /><applet load="1onc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1onc, resolution 1.7Å" /> '''THE REFINED 1.7 ANGST...) |
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| - | [[Image:1onc.jpg|left|200px]]<br /><applet load="1onc" size=" | + | [[Image:1onc.jpg|left|200px]]<br /><applet load="1onc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1onc, resolution 1.7Å" /> | caption="1onc, resolution 1.7Å" /> | ||
'''THE REFINED 1.7 ANGSTROMS X-RAY CRYSTALLOGRAPHIC STRUCTURE OF P-30, AN AMPHIBIAN RIBONUCLEASE WITH ANTI-TUMOR ACTIVITY'''<br /> | '''THE REFINED 1.7 ANGSTROMS X-RAY CRYSTALLOGRAPHIC STRUCTURE OF P-30, AN AMPHIBIAN RIBONUCLEASE WITH ANTI-TUMOR ACTIVITY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystallographic structure of P-30 protein (Onconase) has been | + | The X-ray crystallographic structure of P-30 protein (Onconase) has been solved by multiple isomorphous replacement and the structure has been refined at 1.7 A resolution to a conventional R-factor of 0.178. The molecular model comprises all 826 non-hydrogen protein atoms, 96 solvent molecules and a sulfate anion that is bound at the active site. The molecular structure is similar to that of ribonuclease A. The active site cleft is located at the junction of two three-stranded beta-sheets and the N-terminal helix. A sulfate anion is non-covalently bound by Lys9, His10, His97, Phe98 and an intermolecular contact involving Lys55' from a neighboring molecule. The N-terminal pyroglutamyl (Pyr) residue is part of the active site and its O epsilon 1 atom forms a hydrogen bond with the Lys9 N zeta. The previously constructed comparative molecular model of P-30 based on ribonuclease A correctly predicted the overall fold of P-30 and the conformation of its active site residues. The model failed to predict the conformation of Pyr1 and the conformation of the two loops following helix alpha 3 and strand beta 3. |
==About this Structure== | ==About this Structure== | ||
| - | 1ONC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_pipiens Rana pipiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ONC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rana_pipiens Rana pipiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ardelt, W.]] | [[Category: Ardelt, W.]] | ||
| - | [[Category: James, M | + | [[Category: James, M N.G.]] |
| - | [[Category: Mosimann, S | + | [[Category: Mosimann, S C.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: pancreatic ribonuclease]] | [[Category: pancreatic ribonuclease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:35 2008'' |
Revision as of 12:19, 21 February 2008
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THE REFINED 1.7 ANGSTROMS X-RAY CRYSTALLOGRAPHIC STRUCTURE OF P-30, AN AMPHIBIAN RIBONUCLEASE WITH ANTI-TUMOR ACTIVITY
Overview
The X-ray crystallographic structure of P-30 protein (Onconase) has been solved by multiple isomorphous replacement and the structure has been refined at 1.7 A resolution to a conventional R-factor of 0.178. The molecular model comprises all 826 non-hydrogen protein atoms, 96 solvent molecules and a sulfate anion that is bound at the active site. The molecular structure is similar to that of ribonuclease A. The active site cleft is located at the junction of two three-stranded beta-sheets and the N-terminal helix. A sulfate anion is non-covalently bound by Lys9, His10, His97, Phe98 and an intermolecular contact involving Lys55' from a neighboring molecule. The N-terminal pyroglutamyl (Pyr) residue is part of the active site and its O epsilon 1 atom forms a hydrogen bond with the Lys9 N zeta. The previously constructed comparative molecular model of P-30 based on ribonuclease A correctly predicted the overall fold of P-30 and the conformation of its active site residues. The model failed to predict the conformation of Pyr1 and the conformation of the two loops following helix alpha 3 and strand beta 3.
About this Structure
1ONC is a Single protein structure of sequence from Rana pipiens with as ligand. Full crystallographic information is available from OCA.
Reference
Refined 1.7 A X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity., Mosimann SC, Ardelt W, James MN, J Mol Biol. 1994 Mar 4;236(4):1141-53. PMID:8120892
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