1mrk
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1mrk.gif|left|200px]] | + | [[Image:1mrk.gif|left|200px]] |
| - | + | ||
| - | '''STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS''' | + | {{Structure |
| + | |PDB= 1mrk |SIZE=350|CAPTION= <scene name='initialview01'>1mrk</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FMC:FORMYCIN'>FMC</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MRK is a [ | + | 1MRK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trichosanthes_kirilowii Trichosanthes kirilowii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRK OCA]. |
==Reference== | ==Reference== | ||
| - | Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins., Huang Q, Liu S, Tang Y, Jin S, Wang Y, Biochem J. 1995 Jul 1;309 ( Pt 1):285-98. PMID:[http:// | + | Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins., Huang Q, Liu S, Tang Y, Jin S, Wang Y, Biochem J. 1995 Jul 1;309 ( Pt 1):285-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7619070 7619070] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichosanthes kirilowii]] | [[Category: Trichosanthes kirilowii]] | ||
| Line 21: | Line 30: | ||
[[Category: ribosome-inactivating protein]] | [[Category: ribosome-inactivating protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:47:17 2008'' |
Revision as of 10:47, 20 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS
Overview
Two ribosome-inactivating proteins, trichosanthin and alpha-momorcharin, have been studied in the forms of complexes with ATP or formycin, by an X-ray-crystallographic method at 1.6-2.0 A (0.16-0.20 nm) resolution. The native alpha-momorcharin had been studied at 2.2 A resolution. Structures of trichosanthin were determined by a multiple isomorphous replacement method. Structures of alpha-momorcharin were determined by a molecular replacement method using refined trichosanthin as the searching model. Small ligands in all these complexes have been recognized and built on the difference in electron density. All these structures have been refined to achieve good results, both in terms of crystallography and of ideal geometry. These two proteins show considerable similarity in their three-dimensional folding and to that of related proteins. On the basis of these structures, detailed geometries of the active centres of these two proteins are described and are compared with those of related proteins. In all complexes the interactions between ligand atoms and protein atoms, including hydrophobic forces, aromatic stacking interactions and hydrogen bonds, are found to be specific towards the adenine base. The relationship between the sequence conservation of ribosome-inactivating proteins and their active-centre geometry was analysed. A depurinating mechanism of ribosome-inactivating proteins is proposed on the basis of these results. The N-7 atom of the substrate base group is proposed to be protonated by an acidic residue in the active centre.
About this Structure
1MRK is a Single protein structure of sequence from Trichosanthes kirilowii. Full crystallographic information is available from OCA.
Reference
Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins., Huang Q, Liu S, Tang Y, Jin S, Wang Y, Biochem J. 1995 Jul 1;309 ( Pt 1):285-98. PMID:7619070
Page seeded by OCA on Thu Mar 20 12:47:17 2008
